|
anno_start anno_end anno_text entity_type sentence section |
|
0 9 Structure evidence Structure of the Dual-Mode Wnt Regulator Kremen1 and Insight into Ternary Complex Formation with LRP6 and Dickkopf TITLE |
|
27 30 Wnt protein_type Structure of the Dual-Mode Wnt Regulator Kremen1 and Insight into Ternary Complex Formation with LRP6 and Dickkopf TITLE |
|
41 48 Kremen1 protein Structure of the Dual-Mode Wnt Regulator Kremen1 and Insight into Ternary Complex Formation with LRP6 and Dickkopf TITLE |
|
97 101 LRP6 protein Structure of the Dual-Mode Wnt Regulator Kremen1 and Insight into Ternary Complex Formation with LRP6 and Dickkopf TITLE |
|
106 114 Dickkopf protein_type Structure of the Dual-Mode Wnt Regulator Kremen1 and Insight into Ternary Complex Formation with LRP6 and Dickkopf TITLE |
|
0 14 Kremen 1 and 2 protein_type Kremen 1 and 2 have been identified as co-receptors for Dickkopf (Dkk) proteins, hallmark secreted antagonists of canonical Wnt signaling. ABSTRACT |
|
39 51 co-receptors protein_type Kremen 1 and 2 have been identified as co-receptors for Dickkopf (Dkk) proteins, hallmark secreted antagonists of canonical Wnt signaling. ABSTRACT |
|
56 64 Dickkopf protein_type Kremen 1 and 2 have been identified as co-receptors for Dickkopf (Dkk) proteins, hallmark secreted antagonists of canonical Wnt signaling. ABSTRACT |
|
66 69 Dkk protein_type Kremen 1 and 2 have been identified as co-receptors for Dickkopf (Dkk) proteins, hallmark secreted antagonists of canonical Wnt signaling. ABSTRACT |
|
124 127 Wnt protein_type Kremen 1 and 2 have been identified as co-receptors for Dickkopf (Dkk) proteins, hallmark secreted antagonists of canonical Wnt signaling. ABSTRACT |
|
22 40 crystal structures evidence We present here three crystal structures of the ectodomain of human Kremen1 (KRM1ECD) at resolutions between 1.9 and 3.2Β Γ
. KRM1ECD emerges as a rigid molecule with tight interactions stabilizing a triangular arrangement of its Kringle, WSC, and CUB structural domains. ABSTRACT |
|
48 58 ectodomain structure_element We present here three crystal structures of the ectodomain of human Kremen1 (KRM1ECD) at resolutions between 1.9 and 3.2Β Γ
. KRM1ECD emerges as a rigid molecule with tight interactions stabilizing a triangular arrangement of its Kringle, WSC, and CUB structural domains. ABSTRACT |
|
62 67 human species We present here three crystal structures of the ectodomain of human Kremen1 (KRM1ECD) at resolutions between 1.9 and 3.2Β Γ
. KRM1ECD emerges as a rigid molecule with tight interactions stabilizing a triangular arrangement of its Kringle, WSC, and CUB structural domains. ABSTRACT |
|
68 75 Kremen1 protein We present here three crystal structures of the ectodomain of human Kremen1 (KRM1ECD) at resolutions between 1.9 and 3.2Β Γ
. KRM1ECD emerges as a rigid molecule with tight interactions stabilizing a triangular arrangement of its Kringle, WSC, and CUB structural domains. ABSTRACT |
|
77 81 KRM1 protein We present here three crystal structures of the ectodomain of human Kremen1 (KRM1ECD) at resolutions between 1.9 and 3.2Β Γ
. KRM1ECD emerges as a rigid molecule with tight interactions stabilizing a triangular arrangement of its Kringle, WSC, and CUB structural domains. ABSTRACT |
|
81 84 ECD structure_element We present here three crystal structures of the ectodomain of human Kremen1 (KRM1ECD) at resolutions between 1.9 and 3.2Β Γ
. KRM1ECD emerges as a rigid molecule with tight interactions stabilizing a triangular arrangement of its Kringle, WSC, and CUB structural domains. ABSTRACT |
|
124 128 KRM1 protein We present here three crystal structures of the ectodomain of human Kremen1 (KRM1ECD) at resolutions between 1.9 and 3.2Β Γ
. KRM1ECD emerges as a rigid molecule with tight interactions stabilizing a triangular arrangement of its Kringle, WSC, and CUB structural domains. ABSTRACT |
|
128 131 ECD structure_element We present here three crystal structures of the ectodomain of human Kremen1 (KRM1ECD) at resolutions between 1.9 and 3.2Β Γ
. KRM1ECD emerges as a rigid molecule with tight interactions stabilizing a triangular arrangement of its Kringle, WSC, and CUB structural domains. ABSTRACT |
|
198 220 triangular arrangement protein_state We present here three crystal structures of the ectodomain of human Kremen1 (KRM1ECD) at resolutions between 1.9 and 3.2Β Γ
. KRM1ECD emerges as a rigid molecule with tight interactions stabilizing a triangular arrangement of its Kringle, WSC, and CUB structural domains. ABSTRACT |
|
228 235 Kringle structure_element We present here three crystal structures of the ectodomain of human Kremen1 (KRM1ECD) at resolutions between 1.9 and 3.2Β Γ
. KRM1ECD emerges as a rigid molecule with tight interactions stabilizing a triangular arrangement of its Kringle, WSC, and CUB structural domains. ABSTRACT |
|
237 240 WSC structure_element We present here three crystal structures of the ectodomain of human Kremen1 (KRM1ECD) at resolutions between 1.9 and 3.2Β Γ
. KRM1ECD emerges as a rigid molecule with tight interactions stabilizing a triangular arrangement of its Kringle, WSC, and CUB structural domains. ABSTRACT |
|
246 249 CUB structure_element We present here three crystal structures of the ectodomain of human Kremen1 (KRM1ECD) at resolutions between 1.9 and 3.2Β Γ
. KRM1ECD emerges as a rigid molecule with tight interactions stabilizing a triangular arrangement of its Kringle, WSC, and CUB structural domains. ABSTRACT |
|
4 14 structures evidence The structures reveal an unpredicted homology of the WSC domain to hepatocyte growth factor. ABSTRACT |
|
53 56 WSC structure_element The structures reveal an unpredicted homology of the WSC domain to hepatocyte growth factor. ABSTRACT |
|
67 91 hepatocyte growth factor protein_type The structures reveal an unpredicted homology of the WSC domain to hepatocyte growth factor. ABSTRACT |
|
80 83 Wnt protein_type We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between Ξ²-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD. ABSTRACT |
|
84 95 co-receptor protein_type We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between Ξ²-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD. ABSTRACT |
|
96 102 Lrp5/6 protein_type We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between Ξ²-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD. ABSTRACT |
|
104 107 Dkk protein_type We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between Ξ²-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD. ABSTRACT |
|
113 116 Krm protein_type We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between Ξ²-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD. ABSTRACT |
|
159 176 crystal structure evidence We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between Ξ²-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD. ABSTRACT |
|
185 221 Ξ²-propeller/EGF repeats (PE) 3 and 4 structure_element We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between Ξ²-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD. ABSTRACT |
|
229 232 Wnt protein_type We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between Ξ²-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD. ABSTRACT |
|
233 244 co-receptor protein_type We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between Ξ²-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD. ABSTRACT |
|
245 249 LRP6 protein We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between Ξ²-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD. ABSTRACT |
|
251 255 LRP6 protein We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between Ξ²-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD. ABSTRACT |
|
255 261 PE3PE4 structure_element We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between Ξ²-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD. ABSTRACT |
|
268 290 cysteine-rich domain 2 structure_element We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between Ξ²-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD. ABSTRACT |
|
292 296 CRD2 structure_element We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between Ξ²-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD. ABSTRACT |
|
301 305 DKK1 protein We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between Ξ²-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD. ABSTRACT |
|
311 315 KRM1 protein We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between Ξ²-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD. ABSTRACT |
|
315 318 ECD structure_element We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between Ξ²-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD. ABSTRACT |
|
0 4 DKK1 protein DKK1CRD2 is sandwiched between LRP6PE3 and KRM1Kringle-WSC. ABSTRACT |
|
4 8 CRD2 structure_element DKK1CRD2 is sandwiched between LRP6PE3 and KRM1Kringle-WSC. ABSTRACT |
|
31 35 LRP6 protein DKK1CRD2 is sandwiched between LRP6PE3 and KRM1Kringle-WSC. ABSTRACT |
|
35 38 PE3 structure_element DKK1CRD2 is sandwiched between LRP6PE3 and KRM1Kringle-WSC. ABSTRACT |
|
43 47 KRM1 protein DKK1CRD2 is sandwiched between LRP6PE3 and KRM1Kringle-WSC. ABSTRACT |
|
47 58 Kringle-WSC structure_element DKK1CRD2 is sandwiched between LRP6PE3 and KRM1Kringle-WSC. ABSTRACT |
|
0 8 Modeling experimental_method Modeling studies supported by surface plasmon resonance suggest a direct interaction site between Krm1CUB and Lrp6PE2. ABSTRACT |
|
30 55 surface plasmon resonance experimental_method Modeling studies supported by surface plasmon resonance suggest a direct interaction site between Krm1CUB and Lrp6PE2. ABSTRACT |
|
73 89 interaction site site Modeling studies supported by surface plasmon resonance suggest a direct interaction site between Krm1CUB and Lrp6PE2. ABSTRACT |
|
98 102 Krm1 protein Modeling studies supported by surface plasmon resonance suggest a direct interaction site between Krm1CUB and Lrp6PE2. ABSTRACT |
|
102 105 CUB structure_element Modeling studies supported by surface plasmon resonance suggest a direct interaction site between Krm1CUB and Lrp6PE2. ABSTRACT |
|
110 114 Lrp6 protein Modeling studies supported by surface plasmon resonance suggest a direct interaction site between Krm1CUB and Lrp6PE2. ABSTRACT |
|
114 117 PE2 structure_element Modeling studies supported by surface plasmon resonance suggest a direct interaction site between Krm1CUB and Lrp6PE2. ABSTRACT |
|
4 13 structure evidence The structure of the KREMEN 1 ectodomain is solved from three crystal forms ABSTRACT |
|
21 29 KREMEN 1 protein The structure of the KREMEN 1 ectodomain is solved from three crystal forms ABSTRACT |
|
30 40 ectodomain structure_element The structure of the KREMEN 1 ectodomain is solved from three crystal forms ABSTRACT |
|
44 50 solved experimental_method The structure of the KREMEN 1 ectodomain is solved from three crystal forms ABSTRACT |
|
62 75 crystal forms evidence The structure of the KREMEN 1 ectodomain is solved from three crystal forms ABSTRACT |
|
0 7 Kringle structure_element Kringle, WSC, and CUB subdomains interact tightly to form a single structural unit ABSTRACT |
|
9 12 WSC structure_element Kringle, WSC, and CUB subdomains interact tightly to form a single structural unit ABSTRACT |
|
18 21 CUB structure_element Kringle, WSC, and CUB subdomains interact tightly to form a single structural unit ABSTRACT |
|
4 13 interface site The interface to DKKs is formed from the Kringle and WSC domains ABSTRACT |
|
17 21 DKKs protein_type The interface to DKKs is formed from the Kringle and WSC domains ABSTRACT |
|
41 48 Kringle structure_element The interface to DKKs is formed from the Kringle and WSC domains ABSTRACT |
|
53 56 WSC structure_element The interface to DKKs is formed from the Kringle and WSC domains ABSTRACT |
|
4 7 CUB structure_element The CUB domain is found to interact directly with LRP6PE1PE2 ABSTRACT |
|
50 54 LRP6 protein The CUB domain is found to interact directly with LRP6PE1PE2 ABSTRACT |
|
54 60 PE1PE2 structure_element The CUB domain is found to interact directly with LRP6PE1PE2 ABSTRACT |
|
28 38 ectodomain structure_element Zebisch etΒ al. describe the ectodomain structure of KREMEN 1, a receptor for Wnt antagonists of the DKK family. ABSTRACT |
|
39 48 structure evidence Zebisch etΒ al. describe the ectodomain structure of KREMEN 1, a receptor for Wnt antagonists of the DKK family. ABSTRACT |
|
52 60 KREMEN 1 protein Zebisch etΒ al. describe the ectodomain structure of KREMEN 1, a receptor for Wnt antagonists of the DKK family. ABSTRACT |
|
64 72 receptor protein_type Zebisch etΒ al. describe the ectodomain structure of KREMEN 1, a receptor for Wnt antagonists of the DKK family. ABSTRACT |
|
77 80 Wnt protein_type Zebisch etΒ al. describe the ectodomain structure of KREMEN 1, a receptor for Wnt antagonists of the DKK family. ABSTRACT |
|
100 103 DKK protein_type Zebisch etΒ al. describe the ectodomain structure of KREMEN 1, a receptor for Wnt antagonists of the DKK family. ABSTRACT |
|
0 3 Apo protein_state Apo structures and a complex with functional fragments of DKK1 and LRP6 shed light on the function of this dual-mode regulator of Wnt signaling. ABSTRACT |
|
4 14 structures evidence Apo structures and a complex with functional fragments of DKK1 and LRP6 shed light on the function of this dual-mode regulator of Wnt signaling. ABSTRACT |
|
21 33 complex with protein_state Apo structures and a complex with functional fragments of DKK1 and LRP6 shed light on the function of this dual-mode regulator of Wnt signaling. ABSTRACT |
|
34 54 functional fragments protein_state Apo structures and a complex with functional fragments of DKK1 and LRP6 shed light on the function of this dual-mode regulator of Wnt signaling. ABSTRACT |
|
58 62 DKK1 protein Apo structures and a complex with functional fragments of DKK1 and LRP6 shed light on the function of this dual-mode regulator of Wnt signaling. ABSTRACT |
|
67 71 LRP6 protein Apo structures and a complex with functional fragments of DKK1 and LRP6 shed light on the function of this dual-mode regulator of Wnt signaling. ABSTRACT |
|
130 133 Wnt protein_type Apo structures and a complex with functional fragments of DKK1 and LRP6 shed light on the function of this dual-mode regulator of Wnt signaling. ABSTRACT |
|
13 16 Wnt protein_type Signaling by Wnt morphogens is renowned for its fundamental roles in embryonic development, tissue homeostasis, and stem cell maintenance. INTRO |
|
68 71 Wnt protein_type Due to these functions, generation, delivery, and interpretation of Wnt signals are all heavily regulated in the animal body. INTRO |
|
0 10 Vertebrate taxonomy_domain Vertebrate Dickkopf proteins (Dkk1, 2, and 4) are one of many secreted antagonists of Wnt and function by blocking access to the Wnt co-receptor LRP5/6. INTRO |
|
11 19 Dickkopf protein_type Vertebrate Dickkopf proteins (Dkk1, 2, and 4) are one of many secreted antagonists of Wnt and function by blocking access to the Wnt co-receptor LRP5/6. INTRO |
|
30 34 Dkk1 protein_type Vertebrate Dickkopf proteins (Dkk1, 2, and 4) are one of many secreted antagonists of Wnt and function by blocking access to the Wnt co-receptor LRP5/6. INTRO |
|
36 37 2 protein_type Vertebrate Dickkopf proteins (Dkk1, 2, and 4) are one of many secreted antagonists of Wnt and function by blocking access to the Wnt co-receptor LRP5/6. INTRO |
|
43 44 4 protein_type Vertebrate Dickkopf proteins (Dkk1, 2, and 4) are one of many secreted antagonists of Wnt and function by blocking access to the Wnt co-receptor LRP5/6. INTRO |
|
86 89 Wnt protein_type Vertebrate Dickkopf proteins (Dkk1, 2, and 4) are one of many secreted antagonists of Wnt and function by blocking access to the Wnt co-receptor LRP5/6. INTRO |
|
129 132 Wnt protein_type Vertebrate Dickkopf proteins (Dkk1, 2, and 4) are one of many secreted antagonists of Wnt and function by blocking access to the Wnt co-receptor LRP5/6. INTRO |
|
133 144 co-receptor protein_type Vertebrate Dickkopf proteins (Dkk1, 2, and 4) are one of many secreted antagonists of Wnt and function by blocking access to the Wnt co-receptor LRP5/6. INTRO |
|
145 151 LRP5/6 protein Vertebrate Dickkopf proteins (Dkk1, 2, and 4) are one of many secreted antagonists of Wnt and function by blocking access to the Wnt co-receptor LRP5/6. INTRO |
|
0 6 Kremen protein_type Kremen proteins (Krm1 and Krm2) have been identified as additional high-affinity transmembrane receptors for Dkk. INTRO |
|
17 21 Krm1 protein_type Kremen proteins (Krm1 and Krm2) have been identified as additional high-affinity transmembrane receptors for Dkk. INTRO |
|
26 30 Krm2 protein_type Kremen proteins (Krm1 and Krm2) have been identified as additional high-affinity transmembrane receptors for Dkk. INTRO |
|
81 104 transmembrane receptors protein_type Kremen proteins (Krm1 and Krm2) have been identified as additional high-affinity transmembrane receptors for Dkk. INTRO |
|
109 112 Dkk protein_type Kremen proteins (Krm1 and Krm2) have been identified as additional high-affinity transmembrane receptors for Dkk. INTRO |
|
0 3 Krm protein_type Krm and Dkk synergize in Wnt inhibition during Xenopus embryogenesis to regulate anterior-posterior patterning. INTRO |
|
8 11 Dkk protein_type Krm and Dkk synergize in Wnt inhibition during Xenopus embryogenesis to regulate anterior-posterior patterning. INTRO |
|
25 28 Wnt protein_type Krm and Dkk synergize in Wnt inhibition during Xenopus embryogenesis to regulate anterior-posterior patterning. INTRO |
|
47 54 Xenopus taxonomy_domain Krm and Dkk synergize in Wnt inhibition during Xenopus embryogenesis to regulate anterior-posterior patterning. INTRO |
|
43 54 presence of protein_state Mechanistically it is thought that, in the presence of Dkk, Krm forms a ternary complex with Lrp6, which is then rapidly endocytosed. INTRO |
|
55 58 Dkk protein_type Mechanistically it is thought that, in the presence of Dkk, Krm forms a ternary complex with Lrp6, which is then rapidly endocytosed. INTRO |
|
60 63 Krm protein_type Mechanistically it is thought that, in the presence of Dkk, Krm forms a ternary complex with Lrp6, which is then rapidly endocytosed. INTRO |
|
80 92 complex with protein_state Mechanistically it is thought that, in the presence of Dkk, Krm forms a ternary complex with Lrp6, which is then rapidly endocytosed. INTRO |
|
93 97 Lrp6 protein_type Mechanistically it is thought that, in the presence of Dkk, Krm forms a ternary complex with Lrp6, which is then rapidly endocytosed. INTRO |
|
29 32 Wnt protein_type This amplifies the intrinsic Wnt antagonistic activity of Dkk by efficiently depleting the cell surface of the Wnt co-receptor. INTRO |
|
58 61 Dkk protein_type This amplifies the intrinsic Wnt antagonistic activity of Dkk by efficiently depleting the cell surface of the Wnt co-receptor. INTRO |
|
111 114 Wnt protein_type This amplifies the intrinsic Wnt antagonistic activity of Dkk by efficiently depleting the cell surface of the Wnt co-receptor. INTRO |
|
115 126 co-receptor protein_type This amplifies the intrinsic Wnt antagonistic activity of Dkk by efficiently depleting the cell surface of the Wnt co-receptor. INTRO |
|
25 29 Krm1 protein_type In accordance with this, Krm1β/β and Krm2β/β double knockout mice show a high bone mass phenotype typical of increased Wnt signaling, as well as growth of ectopic forelimb digits. INTRO |
|
37 41 Krm2 protein_type In accordance with this, Krm1β/β and Krm2β/β double knockout mice show a high bone mass phenotype typical of increased Wnt signaling, as well as growth of ectopic forelimb digits. INTRO |
|
45 60 double knockout experimental_method In accordance with this, Krm1β/β and Krm2β/β double knockout mice show a high bone mass phenotype typical of increased Wnt signaling, as well as growth of ectopic forelimb digits. INTRO |
|
61 65 mice taxonomy_domain In accordance with this, Krm1β/β and Krm2β/β double knockout mice show a high bone mass phenotype typical of increased Wnt signaling, as well as growth of ectopic forelimb digits. INTRO |
|
119 122 Wnt protein_type In accordance with this, Krm1β/β and Krm2β/β double knockout mice show a high bone mass phenotype typical of increased Wnt signaling, as well as growth of ectopic forelimb digits. INTRO |
|
69 72 dkk protein_type Growth of ectopic digits is further enhanced upon additional loss of dkk expression. INTRO |
|
4 7 Wnt protein_type The Wnt antagonistic activity of Krm1 is also linked to its importance for correct thymus epithelium formation in mice. INTRO |
|
33 37 Krm1 protein_type The Wnt antagonistic activity of Krm1 is also linked to its importance for correct thymus epithelium formation in mice. INTRO |
|
114 118 mice taxonomy_domain The Wnt antagonistic activity of Krm1 is also linked to its importance for correct thymus epithelium formation in mice. INTRO |
|
18 24 intact protein_state The importance of intact KRM1 for normal human development and health is highlighted by the recent finding that a homozygous mutation in the ectodomain of KRM1 leads to severe ectodermal dysplasia including oligodontia. INTRO |
|
25 29 KRM1 protein The importance of intact KRM1 for normal human development and health is highlighted by the recent finding that a homozygous mutation in the ectodomain of KRM1 leads to severe ectodermal dysplasia including oligodontia. INTRO |
|
41 46 human species The importance of intact KRM1 for normal human development and health is highlighted by the recent finding that a homozygous mutation in the ectodomain of KRM1 leads to severe ectodermal dysplasia including oligodontia. INTRO |
|
141 151 ectodomain structure_element The importance of intact KRM1 for normal human development and health is highlighted by the recent finding that a homozygous mutation in the ectodomain of KRM1 leads to severe ectodermal dysplasia including oligodontia. INTRO |
|
155 159 KRM1 protein The importance of intact KRM1 for normal human development and health is highlighted by the recent finding that a homozygous mutation in the ectodomain of KRM1 leads to severe ectodermal dysplasia including oligodontia. INTRO |
|
19 22 Wnt protein_type Interestingly, the Wnt antagonistic activity of Krm is context dependent, and Krm proteins are actually dual-mode Wnt regulators. INTRO |
|
48 51 Krm protein_type Interestingly, the Wnt antagonistic activity of Krm is context dependent, and Krm proteins are actually dual-mode Wnt regulators. INTRO |
|
78 81 Krm protein_type Interestingly, the Wnt antagonistic activity of Krm is context dependent, and Krm proteins are actually dual-mode Wnt regulators. INTRO |
|
114 117 Wnt protein_type Interestingly, the Wnt antagonistic activity of Krm is context dependent, and Krm proteins are actually dual-mode Wnt regulators. INTRO |
|
7 17 absence of protein_state In the absence of Dkk, Krm1 and 2 change their function from inhibition to enhancement of Lrp6-mediated signaling. INTRO |
|
18 21 Dkk protein_type In the absence of Dkk, Krm1 and 2 change their function from inhibition to enhancement of Lrp6-mediated signaling. INTRO |
|
23 27 Krm1 protein_type In the absence of Dkk, Krm1 and 2 change their function from inhibition to enhancement of Lrp6-mediated signaling. INTRO |
|
32 33 2 protein_type In the absence of Dkk, Krm1 and 2 change their function from inhibition to enhancement of Lrp6-mediated signaling. INTRO |
|
90 94 Lrp6 protein_type In the absence of Dkk, Krm1 and 2 change their function from inhibition to enhancement of Lrp6-mediated signaling. INTRO |
|
21 25 Lrp6 protein_type By direct binding to Lrp6 via the ectodomains, Krm proteins promote Lrp6 cell-surface localization and hence increase receptor availability. INTRO |
|
34 45 ectodomains structure_element By direct binding to Lrp6 via the ectodomains, Krm proteins promote Lrp6 cell-surface localization and hence increase receptor availability. INTRO |
|
47 50 Krm protein_type By direct binding to Lrp6 via the ectodomains, Krm proteins promote Lrp6 cell-surface localization and hence increase receptor availability. INTRO |
|
68 72 Lrp6 protein_type By direct binding to Lrp6 via the ectodomains, Krm proteins promote Lrp6 cell-surface localization and hence increase receptor availability. INTRO |
|
37 40 Krm protein_type Further increasing the complexity of Krm functionality, it was recently found that Krm1 (but not Krm2) can also act independently of LRP5/6 and Wnt as a dependence receptor, triggering apoptosis unless bound to Dkk. INTRO |
|
83 87 Krm1 protein_type Further increasing the complexity of Krm functionality, it was recently found that Krm1 (but not Krm2) can also act independently of LRP5/6 and Wnt as a dependence receptor, triggering apoptosis unless bound to Dkk. INTRO |
|
97 101 Krm2 protein_type Further increasing the complexity of Krm functionality, it was recently found that Krm1 (but not Krm2) can also act independently of LRP5/6 and Wnt as a dependence receptor, triggering apoptosis unless bound to Dkk. INTRO |
|
133 139 LRP5/6 protein Further increasing the complexity of Krm functionality, it was recently found that Krm1 (but not Krm2) can also act independently of LRP5/6 and Wnt as a dependence receptor, triggering apoptosis unless bound to Dkk. INTRO |
|
144 147 Wnt protein_type Further increasing the complexity of Krm functionality, it was recently found that Krm1 (but not Krm2) can also act independently of LRP5/6 and Wnt as a dependence receptor, triggering apoptosis unless bound to Dkk. INTRO |
|
202 210 bound to protein_state Further increasing the complexity of Krm functionality, it was recently found that Krm1 (but not Krm2) can also act independently of LRP5/6 and Wnt as a dependence receptor, triggering apoptosis unless bound to Dkk. INTRO |
|
211 214 Dkk protein_type Further increasing the complexity of Krm functionality, it was recently found that Krm1 (but not Krm2) can also act independently of LRP5/6 and Wnt as a dependence receptor, triggering apoptosis unless bound to Dkk. INTRO |
|
14 18 Krm1 protein_type Structurally, Krm1 and 2 are type I transmembrane proteins with a 40Β kDa ectodomain and a flexible cytoplasmic tail consisting of 60β75 residues. INTRO |
|
23 24 2 protein_type Structurally, Krm1 and 2 are type I transmembrane proteins with a 40Β kDa ectodomain and a flexible cytoplasmic tail consisting of 60β75 residues. INTRO |
|
29 58 type I transmembrane proteins protein_type Structurally, Krm1 and 2 are type I transmembrane proteins with a 40Β kDa ectodomain and a flexible cytoplasmic tail consisting of 60β75 residues. INTRO |
|
73 83 ectodomain structure_element Structurally, Krm1 and 2 are type I transmembrane proteins with a 40Β kDa ectodomain and a flexible cytoplasmic tail consisting of 60β75 residues. INTRO |
|
90 98 flexible protein_state Structurally, Krm1 and 2 are type I transmembrane proteins with a 40Β kDa ectodomain and a flexible cytoplasmic tail consisting of 60β75 residues. INTRO |
|
99 115 cytoplasmic tail structure_element Structurally, Krm1 and 2 are type I transmembrane proteins with a 40Β kDa ectodomain and a flexible cytoplasmic tail consisting of 60β75 residues. INTRO |
|
130 132 60 residue_range Structurally, Krm1 and 2 are type I transmembrane proteins with a 40Β kDa ectodomain and a flexible cytoplasmic tail consisting of 60β75 residues. INTRO |
|
133 135 75 residue_range Structurally, Krm1 and 2 are type I transmembrane proteins with a 40Β kDa ectodomain and a flexible cytoplasmic tail consisting of 60β75 residues. INTRO |
|
4 14 ectodomain structure_element The ectodomain consists of three similarly sized structural domains of around 10Β kDa each: the N-terminal Kringle domain (KR) is followed by a WSC domain of unknown fold. INTRO |
|
106 113 Kringle structure_element The ectodomain consists of three similarly sized structural domains of around 10Β kDa each: the N-terminal Kringle domain (KR) is followed by a WSC domain of unknown fold. INTRO |
|
122 124 KR structure_element The ectodomain consists of three similarly sized structural domains of around 10Β kDa each: the N-terminal Kringle domain (KR) is followed by a WSC domain of unknown fold. INTRO |
|
143 146 WSC structure_element The ectodomain consists of three similarly sized structural domains of around 10Β kDa each: the N-terminal Kringle domain (KR) is followed by a WSC domain of unknown fold. INTRO |
|
33 36 CUB structure_element The third structural domain is a CUB domain. INTRO |
|
3 27 approximately 70-residue residue_range An approximately 70-residue linker connects the CUB domain to the transmembrane span. INTRO |
|
28 34 linker structure_element An approximately 70-residue linker connects the CUB domain to the transmembrane span. INTRO |
|
48 51 CUB structure_element An approximately 70-residue linker connects the CUB domain to the transmembrane span. INTRO |
|
66 84 transmembrane span structure_element An approximately 70-residue linker connects the CUB domain to the transmembrane span. INTRO |
|
3 9 intact protein_state An intact KR-WSC-CUB domain triplet and membrane attachment is required for Wnt antagonism. INTRO |
|
10 20 KR-WSC-CUB structure_element An intact KR-WSC-CUB domain triplet and membrane attachment is required for Wnt antagonism. INTRO |
|
76 79 Wnt protein_type An intact KR-WSC-CUB domain triplet and membrane attachment is required for Wnt antagonism. INTRO |
|
4 22 transmembrane span structure_element The transmembrane span and cytoplasmic tail can be replaced with a GPI linker without impact on Wnt antagonism. INTRO |
|
27 43 cytoplasmic tail structure_element The transmembrane span and cytoplasmic tail can be replaced with a GPI linker without impact on Wnt antagonism. INTRO |
|
67 70 GPI structure_element The transmembrane span and cytoplasmic tail can be replaced with a GPI linker without impact on Wnt antagonism. INTRO |
|
71 77 linker structure_element The transmembrane span and cytoplasmic tail can be replaced with a GPI linker without impact on Wnt antagonism. INTRO |
|
96 99 Wnt protein_type The transmembrane span and cytoplasmic tail can be replaced with a GPI linker without impact on Wnt antagonism. INTRO |
|
4 14 structures evidence The structures presented here reveal the unknown fold of the WSC domain and the tight interactions of all three domains. INTRO |
|
61 64 WSC structure_element The structures presented here reveal the unknown fold of the WSC domain and the tight interactions of all three domains. INTRO |
|
58 85 LRP6PE3PE4-DKK1CRD2-KRM1ECD complex_assembly We further succeeded in determination of a low-resolution LRP6PE3PE4-DKK1CRD2-KRM1ECD complex, defining the architecture of the Wnt inhibitory complex that leads to Lrp6 cell-surface depletion. INTRO |
|
128 131 Wnt protein_type We further succeeded in determination of a low-resolution LRP6PE3PE4-DKK1CRD2-KRM1ECD complex, defining the architecture of the Wnt inhibitory complex that leads to Lrp6 cell-surface depletion. INTRO |
|
132 150 inhibitory complex complex_assembly We further succeeded in determination of a low-resolution LRP6PE3PE4-DKK1CRD2-KRM1ECD complex, defining the architecture of the Wnt inhibitory complex that leads to Lrp6 cell-surface depletion. INTRO |
|
165 169 Lrp6 protein We further succeeded in determination of a low-resolution LRP6PE3PE4-DKK1CRD2-KRM1ECD complex, defining the architecture of the Wnt inhibitory complex that leads to Lrp6 cell-surface depletion. INTRO |
|
34 54 extracellular domain structure_element The recombinant production of the extracellular domain of Krm for structural studies proved challenging (see Experimental Procedures). RESULTS |
|
58 61 Krm protein_type The recombinant production of the extracellular domain of Krm for structural studies proved challenging (see Experimental Procedures). RESULTS |
|
66 84 structural studies experimental_method The recombinant production of the extracellular domain of Krm for structural studies proved challenging (see Experimental Procedures). RESULTS |
|
26 30 KRM1 protein We succeeded in purifying KRM1ECD complexes with DKK1fl, DKK1Linker-CRD2, and DKK1CRD2 that were monodisperse and stable in gel filtration, hence indicating at least micromolar affinity (data not shown). RESULTS |
|
30 33 ECD structure_element We succeeded in purifying KRM1ECD complexes with DKK1fl, DKK1Linker-CRD2, and DKK1CRD2 that were monodisperse and stable in gel filtration, hence indicating at least micromolar affinity (data not shown). RESULTS |
|
34 48 complexes with protein_state We succeeded in purifying KRM1ECD complexes with DKK1fl, DKK1Linker-CRD2, and DKK1CRD2 that were monodisperse and stable in gel filtration, hence indicating at least micromolar affinity (data not shown). RESULTS |
|
49 55 DKK1fl protein We succeeded in purifying KRM1ECD complexes with DKK1fl, DKK1Linker-CRD2, and DKK1CRD2 that were monodisperse and stable in gel filtration, hence indicating at least micromolar affinity (data not shown). RESULTS |
|
57 61 DKK1 protein We succeeded in purifying KRM1ECD complexes with DKK1fl, DKK1Linker-CRD2, and DKK1CRD2 that were monodisperse and stable in gel filtration, hence indicating at least micromolar affinity (data not shown). RESULTS |
|
61 72 Linker-CRD2 structure_element We succeeded in purifying KRM1ECD complexes with DKK1fl, DKK1Linker-CRD2, and DKK1CRD2 that were monodisperse and stable in gel filtration, hence indicating at least micromolar affinity (data not shown). RESULTS |
|
78 82 DKK1 protein We succeeded in purifying KRM1ECD complexes with DKK1fl, DKK1Linker-CRD2, and DKK1CRD2 that were monodisperse and stable in gel filtration, hence indicating at least micromolar affinity (data not shown). RESULTS |
|
82 86 CRD2 structure_element We succeeded in purifying KRM1ECD complexes with DKK1fl, DKK1Linker-CRD2, and DKK1CRD2 that were monodisperse and stable in gel filtration, hence indicating at least micromolar affinity (data not shown). RESULTS |
|
124 138 gel filtration experimental_method We succeeded in purifying KRM1ECD complexes with DKK1fl, DKK1Linker-CRD2, and DKK1CRD2 that were monodisperse and stable in gel filtration, hence indicating at least micromolar affinity (data not shown). RESULTS |
|
8 21 crystal forms evidence Several crystal forms were obtained from these complexes, however, crystals always contained only KRM1 protein. RESULTS |
|
67 75 crystals evidence Several crystal forms were obtained from these complexes, however, crystals always contained only KRM1 protein. RESULTS |
|
98 102 KRM1 protein Several crystal forms were obtained from these complexes, however, crystals always contained only KRM1 protein. RESULTS |
|
3 9 solved experimental_method We solved the structure of KRM1ECD in three crystal forms at 1.9, 2.8, and 3.2Β Γ
resolution (Table 1). RESULTS |
|
14 23 structure evidence We solved the structure of KRM1ECD in three crystal forms at 1.9, 2.8, and 3.2Β Γ
resolution (Table 1). RESULTS |
|
27 31 KRM1 protein We solved the structure of KRM1ECD in three crystal forms at 1.9, 2.8, and 3.2Β Γ
resolution (Table 1). RESULTS |
|
31 34 ECD structure_element We solved the structure of KRM1ECD in three crystal forms at 1.9, 2.8, and 3.2Β Γ
resolution (Table 1). RESULTS |
|
20 29 structure evidence The high-resolution structure is a near full-length model (FigureΒ 1). RESULTS |
|
40 51 full-length protein_state The high-resolution structure is a near full-length model (FigureΒ 1). RESULTS |
|
4 9 small protein_state The small, flexible, and charged 98AEHED102 loop could only be modeled in a slightly lower resolution structure and in crystal form III. RESULTS |
|
11 19 flexible protein_state The small, flexible, and charged 98AEHED102 loop could only be modeled in a slightly lower resolution structure and in crystal form III. RESULTS |
|
25 32 charged protein_state The small, flexible, and charged 98AEHED102 loop could only be modeled in a slightly lower resolution structure and in crystal form III. RESULTS |
|
33 48 98AEHED102 loop structure_element The small, flexible, and charged 98AEHED102 loop could only be modeled in a slightly lower resolution structure and in crystal form III. RESULTS |
|
102 111 structure evidence The small, flexible, and charged 98AEHED102 loop could only be modeled in a slightly lower resolution structure and in crystal form III. RESULTS |
|
4 6 KR structure_element The KR, WSC, and CUB are arranged in a roughly triangular fashion with tight interactions between all three domains. RESULTS |
|
8 11 WSC structure_element The KR, WSC, and CUB are arranged in a roughly triangular fashion with tight interactions between all three domains. RESULTS |
|
17 20 CUB structure_element The KR, WSC, and CUB are arranged in a roughly triangular fashion with tight interactions between all three domains. RESULTS |
|
4 6 KR structure_element The KR domain, which bears two of the four glycosylation sites, contains the canonical three disulfide bridges (C32-C114, C55-C95, C84-C109) and, like other Kringle domains, is low in secondary structure elements. RESULTS |
|
43 62 glycosylation sites site The KR domain, which bears two of the four glycosylation sites, contains the canonical three disulfide bridges (C32-C114, C55-C95, C84-C109) and, like other Kringle domains, is low in secondary structure elements. RESULTS |
|
93 110 disulfide bridges ptm The KR domain, which bears two of the four glycosylation sites, contains the canonical three disulfide bridges (C32-C114, C55-C95, C84-C109) and, like other Kringle domains, is low in secondary structure elements. RESULTS |
|
112 115 C32 residue_name_number The KR domain, which bears two of the four glycosylation sites, contains the canonical three disulfide bridges (C32-C114, C55-C95, C84-C109) and, like other Kringle domains, is low in secondary structure elements. RESULTS |
|
116 120 C114 residue_name_number The KR domain, which bears two of the four glycosylation sites, contains the canonical three disulfide bridges (C32-C114, C55-C95, C84-C109) and, like other Kringle domains, is low in secondary structure elements. RESULTS |
|
122 125 C55 residue_name_number The KR domain, which bears two of the four glycosylation sites, contains the canonical three disulfide bridges (C32-C114, C55-C95, C84-C109) and, like other Kringle domains, is low in secondary structure elements. RESULTS |
|
126 129 C95 residue_name_number The KR domain, which bears two of the four glycosylation sites, contains the canonical three disulfide bridges (C32-C114, C55-C95, C84-C109) and, like other Kringle domains, is low in secondary structure elements. RESULTS |
|
131 134 C84 residue_name_number The KR domain, which bears two of the four glycosylation sites, contains the canonical three disulfide bridges (C32-C114, C55-C95, C84-C109) and, like other Kringle domains, is low in secondary structure elements. RESULTS |
|
135 139 C109 residue_name_number The KR domain, which bears two of the four glycosylation sites, contains the canonical three disulfide bridges (C32-C114, C55-C95, C84-C109) and, like other Kringle domains, is low in secondary structure elements. RESULTS |
|
157 164 Kringle structure_element The KR domain, which bears two of the four glycosylation sites, contains the canonical three disulfide bridges (C32-C114, C55-C95, C84-C109) and, like other Kringle domains, is low in secondary structure elements. RESULTS |
|
30 37 Kringle structure_element The structurally most similar Kringle domain is that of human plasminogen (PDB: 1PKR) with an root-mean-square deviation (RMSD) of 1.7Β Γ
for 73 aligned CΞ± (FigureΒ 1B). RESULTS |
|
56 61 human species The structurally most similar Kringle domain is that of human plasminogen (PDB: 1PKR) with an root-mean-square deviation (RMSD) of 1.7Β Γ
for 73 aligned CΞ± (FigureΒ 1B). RESULTS |
|
62 73 plasminogen protein The structurally most similar Kringle domain is that of human plasminogen (PDB: 1PKR) with an root-mean-square deviation (RMSD) of 1.7Β Γ
for 73 aligned CΞ± (FigureΒ 1B). RESULTS |
|
94 120 root-mean-square deviation evidence The structurally most similar Kringle domain is that of human plasminogen (PDB: 1PKR) with an root-mean-square deviation (RMSD) of 1.7Β Γ
for 73 aligned CΞ± (FigureΒ 1B). RESULTS |
|
122 126 RMSD evidence The structurally most similar Kringle domain is that of human plasminogen (PDB: 1PKR) with an root-mean-square deviation (RMSD) of 1.7Β Γ
for 73 aligned CΞ± (FigureΒ 1B). RESULTS |
|
4 8 KRM1 protein The KRM1 structure reveals the fold of the WSC domain for the first time. RESULTS |
|
9 18 structure evidence The KRM1 structure reveals the fold of the WSC domain for the first time. RESULTS |
|
43 46 WSC structure_element The KRM1 structure reveals the fold of the WSC domain for the first time. RESULTS |
|
4 13 structure evidence The structure is best described as a sandwich of a Ξ²1-Ξ²5-Ξ²3-Ξ²4-Ξ²2 antiparallel Ξ² sheet and a single Ξ± helix. RESULTS |
|
37 45 sandwich structure_element The structure is best described as a sandwich of a Ξ²1-Ξ²5-Ξ²3-Ξ²4-Ξ²2 antiparallel Ξ² sheet and a single Ξ± helix. RESULTS |
|
51 86 Ξ²1-Ξ²5-Ξ²3-Ξ²4-Ξ²2 antiparallel Ξ² sheet structure_element The structure is best described as a sandwich of a Ξ²1-Ξ²5-Ξ²3-Ξ²4-Ξ²2 antiparallel Ξ² sheet and a single Ξ± helix. RESULTS |
|
100 107 Ξ± helix structure_element The structure is best described as a sandwich of a Ξ²1-Ξ²5-Ξ²3-Ξ²4-Ξ²2 antiparallel Ξ² sheet and a single Ξ± helix. RESULTS |
|
4 13 structure evidence The structure is also rich in loops and is stabilized by four disulfide bridges (C122-C186, C147-C167, C151-C169, C190-C198). RESULTS |
|
30 35 loops structure_element The structure is also rich in loops and is stabilized by four disulfide bridges (C122-C186, C147-C167, C151-C169, C190-C198). RESULTS |
|
62 79 disulfide bridges ptm The structure is also rich in loops and is stabilized by four disulfide bridges (C122-C186, C147-C167, C151-C169, C190-C198). RESULTS |
|
81 85 C122 residue_name_number The structure is also rich in loops and is stabilized by four disulfide bridges (C122-C186, C147-C167, C151-C169, C190-C198). RESULTS |
|
86 90 C186 residue_name_number The structure is also rich in loops and is stabilized by four disulfide bridges (C122-C186, C147-C167, C151-C169, C190-C198). RESULTS |
|
92 96 C147 residue_name_number The structure is also rich in loops and is stabilized by four disulfide bridges (C122-C186, C147-C167, C151-C169, C190-C198). RESULTS |
|
97 101 C167 residue_name_number The structure is also rich in loops and is stabilized by four disulfide bridges (C122-C186, C147-C167, C151-C169, C190-C198). RESULTS |
|
103 107 C151 residue_name_number The structure is also rich in loops and is stabilized by four disulfide bridges (C122-C186, C147-C167, C151-C169, C190-C198). RESULTS |
|
108 112 C169 residue_name_number The structure is also rich in loops and is stabilized by four disulfide bridges (C122-C186, C147-C167, C151-C169, C190-C198). RESULTS |
|
114 118 C190 residue_name_number The structure is also rich in loops and is stabilized by four disulfide bridges (C122-C186, C147-C167, C151-C169, C190-C198). RESULTS |
|
119 123 C198 residue_name_number The structure is also rich in loops and is stabilized by four disulfide bridges (C122-C186, C147-C167, C151-C169, C190-C198). RESULTS |
|
10 25 PDBeFold server experimental_method Using the PDBeFold server, we detected a surprising yet significant homology to PAN module domains. RESULTS |
|
80 98 PAN module domains structure_element Using the PDBeFold server, we detected a surprising yet significant homology to PAN module domains. RESULTS |
|
35 59 hepatocyte growth factor protein_type The closest structural relative is hepatocyte growth factor (HGF, PDB: 1GP9), which superposes with an RMSD of 2.3Β Γ
for 58 aligned CΞ± (FigureΒ 1B). RESULTS |
|
61 64 HGF protein_type The closest structural relative is hepatocyte growth factor (HGF, PDB: 1GP9), which superposes with an RMSD of 2.3Β Γ
for 58 aligned CΞ± (FigureΒ 1B). RESULTS |
|
84 94 superposes experimental_method The closest structural relative is hepatocyte growth factor (HGF, PDB: 1GP9), which superposes with an RMSD of 2.3Β Γ
for 58 aligned CΞ± (FigureΒ 1B). RESULTS |
|
103 107 RMSD evidence The closest structural relative is hepatocyte growth factor (HGF, PDB: 1GP9), which superposes with an RMSD of 2.3Β Γ
for 58 aligned CΞ± (FigureΒ 1B). RESULTS |
|
4 7 CUB structure_element The CUB domain bears two glycosylation sites. RESULTS |
|
25 44 glycosylation sites site The CUB domain bears two glycosylation sites. RESULTS |
|
37 53 electron density evidence Although present, the quality of the electron density around N217 did not allow modeling of the sugar moiety. RESULTS |
|
61 65 N217 residue_name_number Although present, the quality of the electron density around N217 did not allow modeling of the sugar moiety. RESULTS |
|
3 17 crystal form I evidence In crystal form I, a calcium ion is present at the canonical position coordinated by the carboxylates of D263, D266 (bidentate), and D306, as well as the carbonyl of N309 and a water molecule. RESULTS |
|
21 28 calcium chemical In crystal form I, a calcium ion is present at the canonical position coordinated by the carboxylates of D263, D266 (bidentate), and D306, as well as the carbonyl of N309 and a water molecule. RESULTS |
|
70 84 coordinated by bond_interaction In crystal form I, a calcium ion is present at the canonical position coordinated by the carboxylates of D263, D266 (bidentate), and D306, as well as the carbonyl of N309 and a water molecule. RESULTS |
|
105 109 D263 residue_name_number In crystal form I, a calcium ion is present at the canonical position coordinated by the carboxylates of D263, D266 (bidentate), and D306, as well as the carbonyl of N309 and a water molecule. RESULTS |
|
111 115 D266 residue_name_number In crystal form I, a calcium ion is present at the canonical position coordinated by the carboxylates of D263, D266 (bidentate), and D306, as well as the carbonyl of N309 and a water molecule. RESULTS |
|
133 137 D306 residue_name_number In crystal form I, a calcium ion is present at the canonical position coordinated by the carboxylates of D263, D266 (bidentate), and D306, as well as the carbonyl of N309 and a water molecule. RESULTS |
|
166 170 N309 residue_name_number In crystal form I, a calcium ion is present at the canonical position coordinated by the carboxylates of D263, D266 (bidentate), and D306, as well as the carbonyl of N309 and a water molecule. RESULTS |
|
177 182 water chemical In crystal form I, a calcium ion is present at the canonical position coordinated by the carboxylates of D263, D266 (bidentate), and D306, as well as the carbonyl of N309 and a water molecule. RESULTS |
|
4 23 coordination sphere site The coordination sphere deviates significantly from perfectly octahedral (not shown). RESULTS |
|
72 79 calcium chemical This might result in the site having a low affinity and may explain why calcium is not present in the two low-resolution crystal forms. RESULTS |
|
121 134 crystal forms evidence This might result in the site having a low affinity and may explain why calcium is not present in the two low-resolution crystal forms. RESULTS |
|
0 7 Loss of protein_state Loss of calcium has led to loop rearrangements and partial disorder in these crystal forms. RESULTS |
|
8 15 calcium chemical Loss of calcium has led to loop rearrangements and partial disorder in these crystal forms. RESULTS |
|
27 31 loop structure_element Loss of calcium has led to loop rearrangements and partial disorder in these crystal forms. RESULTS |
|
77 90 crystal forms evidence Loss of calcium has led to loop rearrangements and partial disorder in these crystal forms. RESULTS |
|
39 44 CUB_C structure_element The closest structural relative is the CUB_C domain of Tsg-6 (PDB: 2WNO), which superposes with KRMCUB with an RMSD of 1.6Β Γ
for 104 CΞ± (FigureΒ 1B). RESULTS |
|
55 60 Tsg-6 protein The closest structural relative is the CUB_C domain of Tsg-6 (PDB: 2WNO), which superposes with KRMCUB with an RMSD of 1.6Β Γ
for 104 CΞ± (FigureΒ 1B). RESULTS |
|
80 90 superposes experimental_method The closest structural relative is the CUB_C domain of Tsg-6 (PDB: 2WNO), which superposes with KRMCUB with an RMSD of 1.6Β Γ
for 104 CΞ± (FigureΒ 1B). RESULTS |
|
96 99 KRM protein The closest structural relative is the CUB_C domain of Tsg-6 (PDB: 2WNO), which superposes with KRMCUB with an RMSD of 1.6Β Γ
for 104 CΞ± (FigureΒ 1B). RESULTS |
|
99 102 CUB structure_element The closest structural relative is the CUB_C domain of Tsg-6 (PDB: 2WNO), which superposes with KRMCUB with an RMSD of 1.6Β Γ
for 104 CΞ± (FigureΒ 1B). RESULTS |
|
111 115 RMSD evidence The closest structural relative is the CUB_C domain of Tsg-6 (PDB: 2WNO), which superposes with KRMCUB with an RMSD of 1.6Β Γ
for 104 CΞ± (FigureΒ 1B). RESULTS |
|
2 15 superposition experimental_method A superposition of the three KRM1 structures reveals no major structural differences (FigureΒ 1C) as anticipated from the plethora of interactions between the three domains. RESULTS |
|
29 33 KRM1 protein A superposition of the three KRM1 structures reveals no major structural differences (FigureΒ 1C) as anticipated from the plethora of interactions between the three domains. RESULTS |
|
34 44 structures evidence A superposition of the three KRM1 structures reveals no major structural differences (FigureΒ 1C) as anticipated from the plethora of interactions between the three domains. RESULTS |
|
52 69 Ca2+ binding site site Minor differences are caused by the collapse of the Ca2+ binding site in crystal forms II and III and loop flexibility in the KR domain. RESULTS |
|
73 97 crystal forms II and III evidence Minor differences are caused by the collapse of the Ca2+ binding site in crystal forms II and III and loop flexibility in the KR domain. RESULTS |
|
102 106 loop structure_element Minor differences are caused by the collapse of the Ca2+ binding site in crystal forms II and III and loop flexibility in the KR domain. RESULTS |
|
126 128 KR structure_element Minor differences are caused by the collapse of the Ca2+ binding site in crystal forms II and III and loop flexibility in the KR domain. RESULTS |
|
4 9 F207S mutant The F207S mutation recently found to cause ectodermal dysplasia in Palestinian families maps to the hydrophobic core of the protein at the interface of the three subdomains (FigureΒ 1A). RESULTS |
|
100 116 hydrophobic core site The F207S mutation recently found to cause ectodermal dysplasia in Palestinian families maps to the hydrophobic core of the protein at the interface of the three subdomains (FigureΒ 1A). RESULTS |
|
139 148 interface site The F207S mutation recently found to cause ectodermal dysplasia in Palestinian families maps to the hydrophobic core of the protein at the interface of the three subdomains (FigureΒ 1A). RESULTS |
|
19 27 bound to protein_state Such a mutation is bound to severely destabilize the protein structure of KRM1, leading to disturbance of its Wnt antagonistic, Wnt stimulatory, and Wnt independent activity. RESULTS |
|
74 78 KRM1 protein Such a mutation is bound to severely destabilize the protein structure of KRM1, leading to disturbance of its Wnt antagonistic, Wnt stimulatory, and Wnt independent activity. RESULTS |
|
110 113 Wnt protein_type Such a mutation is bound to severely destabilize the protein structure of KRM1, leading to disturbance of its Wnt antagonistic, Wnt stimulatory, and Wnt independent activity. RESULTS |
|
128 131 Wnt protein_type Such a mutation is bound to severely destabilize the protein structure of KRM1, leading to disturbance of its Wnt antagonistic, Wnt stimulatory, and Wnt independent activity. RESULTS |
|
149 152 Wnt protein_type Such a mutation is bound to severely destabilize the protein structure of KRM1, leading to disturbance of its Wnt antagonistic, Wnt stimulatory, and Wnt independent activity. RESULTS |
|
0 18 Co-crystallization experimental_method Co-crystallization of LRP6PE3PE4 with DKK1CRD2, and LRP6PE1 with an N-terminal peptide of DKK1 has provided valuable structural insight into direct Wnt inhibition by Dkk ligands. RESULTS |
|
22 26 LRP6 protein Co-crystallization of LRP6PE3PE4 with DKK1CRD2, and LRP6PE1 with an N-terminal peptide of DKK1 has provided valuable structural insight into direct Wnt inhibition by Dkk ligands. RESULTS |
|
26 32 PE3PE4 structure_element Co-crystallization of LRP6PE3PE4 with DKK1CRD2, and LRP6PE1 with an N-terminal peptide of DKK1 has provided valuable structural insight into direct Wnt inhibition by Dkk ligands. RESULTS |
|
38 42 DKK1 protein Co-crystallization of LRP6PE3PE4 with DKK1CRD2, and LRP6PE1 with an N-terminal peptide of DKK1 has provided valuable structural insight into direct Wnt inhibition by Dkk ligands. RESULTS |
|
42 46 CRD2 structure_element Co-crystallization of LRP6PE3PE4 with DKK1CRD2, and LRP6PE1 with an N-terminal peptide of DKK1 has provided valuable structural insight into direct Wnt inhibition by Dkk ligands. RESULTS |
|
52 56 LRP6 protein Co-crystallization of LRP6PE3PE4 with DKK1CRD2, and LRP6PE1 with an N-terminal peptide of DKK1 has provided valuable structural insight into direct Wnt inhibition by Dkk ligands. RESULTS |
|
56 59 PE1 structure_element Co-crystallization of LRP6PE3PE4 with DKK1CRD2, and LRP6PE1 with an N-terminal peptide of DKK1 has provided valuable structural insight into direct Wnt inhibition by Dkk ligands. RESULTS |
|
90 94 DKK1 protein Co-crystallization of LRP6PE3PE4 with DKK1CRD2, and LRP6PE1 with an N-terminal peptide of DKK1 has provided valuable structural insight into direct Wnt inhibition by Dkk ligands. RESULTS |
|
148 151 Wnt protein_type Co-crystallization of LRP6PE3PE4 with DKK1CRD2, and LRP6PE1 with an N-terminal peptide of DKK1 has provided valuable structural insight into direct Wnt inhibition by Dkk ligands. RESULTS |
|
166 169 Dkk protein_type Co-crystallization of LRP6PE3PE4 with DKK1CRD2, and LRP6PE1 with an N-terminal peptide of DKK1 has provided valuable structural insight into direct Wnt inhibition by Dkk ligands. RESULTS |
|
23 27 flat protein_state One face of the rather flat DKK1CRD2 fragment binds to the third Ξ² propeller of LRP6. RESULTS |
|
28 32 DKK1 protein One face of the rather flat DKK1CRD2 fragment binds to the third Ξ² propeller of LRP6. RESULTS |
|
32 36 CRD2 structure_element One face of the rather flat DKK1CRD2 fragment binds to the third Ξ² propeller of LRP6. RESULTS |
|
46 54 binds to protein_state One face of the rather flat DKK1CRD2 fragment binds to the third Ξ² propeller of LRP6. RESULTS |
|
59 76 third Ξ² propeller structure_element One face of the rather flat DKK1CRD2 fragment binds to the third Ξ² propeller of LRP6. RESULTS |
|
80 84 LRP6 protein One face of the rather flat DKK1CRD2 fragment binds to the third Ξ² propeller of LRP6. RESULTS |
|
0 19 Mutational analyses experimental_method Mutational analyses further implied that the LRP6PE3-averted face of DKK1CRD2 bears the Krm binding site, hence suggesting how Dkk can recruit both receptors into a ternary complex. RESULTS |
|
45 49 LRP6 protein Mutational analyses further implied that the LRP6PE3-averted face of DKK1CRD2 bears the Krm binding site, hence suggesting how Dkk can recruit both receptors into a ternary complex. RESULTS |
|
49 52 PE3 structure_element Mutational analyses further implied that the LRP6PE3-averted face of DKK1CRD2 bears the Krm binding site, hence suggesting how Dkk can recruit both receptors into a ternary complex. RESULTS |
|
69 73 DKK1 protein Mutational analyses further implied that the LRP6PE3-averted face of DKK1CRD2 bears the Krm binding site, hence suggesting how Dkk can recruit both receptors into a ternary complex. RESULTS |
|
73 77 CRD2 structure_element Mutational analyses further implied that the LRP6PE3-averted face of DKK1CRD2 bears the Krm binding site, hence suggesting how Dkk can recruit both receptors into a ternary complex. RESULTS |
|
88 104 Krm binding site site Mutational analyses further implied that the LRP6PE3-averted face of DKK1CRD2 bears the Krm binding site, hence suggesting how Dkk can recruit both receptors into a ternary complex. RESULTS |
|
127 130 Dkk protein_type Mutational analyses further implied that the LRP6PE3-averted face of DKK1CRD2 bears the Krm binding site, hence suggesting how Dkk can recruit both receptors into a ternary complex. RESULTS |
|
148 157 receptors protein_type Mutational analyses further implied that the LRP6PE3-averted face of DKK1CRD2 bears the Krm binding site, hence suggesting how Dkk can recruit both receptors into a ternary complex. RESULTS |
|
59 65 Lrp5/6 protein_type To obtain direct insight into ternary complex formation by Lrp5/6, Dkk, and Krm, we subjected an LRP6PE3PE4-DKK1fl-KRM1ECD complex to crystallization trials. RESULTS |
|
67 70 Dkk protein_type To obtain direct insight into ternary complex formation by Lrp5/6, Dkk, and Krm, we subjected an LRP6PE3PE4-DKK1fl-KRM1ECD complex to crystallization trials. RESULTS |
|
76 79 Krm protein_type To obtain direct insight into ternary complex formation by Lrp5/6, Dkk, and Krm, we subjected an LRP6PE3PE4-DKK1fl-KRM1ECD complex to crystallization trials. RESULTS |
|
97 122 LRP6PE3PE4-DKK1fl-KRM1ECD complex_assembly To obtain direct insight into ternary complex formation by Lrp5/6, Dkk, and Krm, we subjected an LRP6PE3PE4-DKK1fl-KRM1ECD complex to crystallization trials. RESULTS |
|
134 156 crystallization trials experimental_method To obtain direct insight into ternary complex formation by Lrp5/6, Dkk, and Krm, we subjected an LRP6PE3PE4-DKK1fl-KRM1ECD complex to crystallization trials. RESULTS |
|
0 16 Diffraction data evidence Diffraction data collected from the resulting crystals were highly anisotropic with diffraction extending in the best directions to 3.5Β Γ
and 3.7Β Γ
but only to 6.4Β Γ
in the third direction. RESULTS |
|
46 54 crystals evidence Diffraction data collected from the resulting crystals were highly anisotropic with diffraction extending in the best directions to 3.5Β Γ
and 3.7Β Γ
but only to 6.4Β Γ
in the third direction. RESULTS |
|
36 47 diffraction evidence Despite the lack of high-resolution diffraction, the general architecture of the ternary complex is revealed (FigureΒ 2A). RESULTS |
|
0 4 DKK1 protein DKK1CRD2 binds to the top face of the LRP6 PE3 Ξ² propeller as described earlier for the binary complex. RESULTS |
|
4 8 CRD2 structure_element DKK1CRD2 binds to the top face of the LRP6 PE3 Ξ² propeller as described earlier for the binary complex. RESULTS |
|
9 17 binds to protein_state DKK1CRD2 binds to the top face of the LRP6 PE3 Ξ² propeller as described earlier for the binary complex. RESULTS |
|
38 42 LRP6 protein DKK1CRD2 binds to the top face of the LRP6 PE3 Ξ² propeller as described earlier for the binary complex. RESULTS |
|
43 46 PE3 structure_element DKK1CRD2 binds to the top face of the LRP6 PE3 Ξ² propeller as described earlier for the binary complex. RESULTS |
|
47 58 Ξ² propeller structure_element DKK1CRD2 binds to the top face of the LRP6 PE3 Ξ² propeller as described earlier for the binary complex. RESULTS |
|
0 4 KRM1 protein KRM1ECD does indeed bind on the opposite side of DKK1CRD2 with only its KR and WSC domains engaged in binding (FigureΒ 2A). RESULTS |
|
4 7 ECD structure_element KRM1ECD does indeed bind on the opposite side of DKK1CRD2 with only its KR and WSC domains engaged in binding (FigureΒ 2A). RESULTS |
|
20 27 bind on protein_state KRM1ECD does indeed bind on the opposite side of DKK1CRD2 with only its KR and WSC domains engaged in binding (FigureΒ 2A). RESULTS |
|
49 53 DKK1 protein KRM1ECD does indeed bind on the opposite side of DKK1CRD2 with only its KR and WSC domains engaged in binding (FigureΒ 2A). RESULTS |
|
53 57 CRD2 structure_element KRM1ECD does indeed bind on the opposite side of DKK1CRD2 with only its KR and WSC domains engaged in binding (FigureΒ 2A). RESULTS |
|
72 74 KR structure_element KRM1ECD does indeed bind on the opposite side of DKK1CRD2 with only its KR and WSC domains engaged in binding (FigureΒ 2A). RESULTS |
|
79 82 WSC structure_element KRM1ECD does indeed bind on the opposite side of DKK1CRD2 with only its KR and WSC domains engaged in binding (FigureΒ 2A). RESULTS |
|
45 60 crystallization experimental_method Although present in the complex subjected to crystallization, we observe no density that could correspond to CRD1 or the domain linkerΒ (L). RESULTS |
|
76 83 density evidence Although present in the complex subjected to crystallization, we observe no density that could correspond to CRD1 or the domain linkerΒ (L). RESULTS |
|
109 113 CRD1 structure_element Although present in the complex subjected to crystallization, we observe no density that could correspond to CRD1 or the domain linkerΒ (L). RESULTS |
|
121 134 domain linker structure_element Although present in the complex subjected to crystallization, we observe no density that could correspond to CRD1 or the domain linkerΒ (L). RESULTS |
|
136 137 L structure_element Although present in the complex subjected to crystallization, we observe no density that could correspond to CRD1 or the domain linkerΒ (L). RESULTS |
|
20 24 CRD2 structure_element We confirm that the CRD2 of DKK1 is required and sufficient for binding to KRM1: In surface plasmon resonance (SPR), we measured low micromolar affinity between full-length DKK1 and immobilized KRM1ECD (FigureΒ 2B). RESULTS |
|
28 32 DKK1 protein We confirm that the CRD2 of DKK1 is required and sufficient for binding to KRM1: In surface plasmon resonance (SPR), we measured low micromolar affinity between full-length DKK1 and immobilized KRM1ECD (FigureΒ 2B). RESULTS |
|
75 79 KRM1 protein We confirm that the CRD2 of DKK1 is required and sufficient for binding to KRM1: In surface plasmon resonance (SPR), we measured low micromolar affinity between full-length DKK1 and immobilized KRM1ECD (FigureΒ 2B). RESULTS |
|
84 109 surface plasmon resonance experimental_method We confirm that the CRD2 of DKK1 is required and sufficient for binding to KRM1: In surface plasmon resonance (SPR), we measured low micromolar affinity between full-length DKK1 and immobilized KRM1ECD (FigureΒ 2B). RESULTS |
|
111 114 SPR experimental_method We confirm that the CRD2 of DKK1 is required and sufficient for binding to KRM1: In surface plasmon resonance (SPR), we measured low micromolar affinity between full-length DKK1 and immobilized KRM1ECD (FigureΒ 2B). RESULTS |
|
144 152 affinity evidence We confirm that the CRD2 of DKK1 is required and sufficient for binding to KRM1: In surface plasmon resonance (SPR), we measured low micromolar affinity between full-length DKK1 and immobilized KRM1ECD (FigureΒ 2B). RESULTS |
|
161 172 full-length protein_state We confirm that the CRD2 of DKK1 is required and sufficient for binding to KRM1: In surface plasmon resonance (SPR), we measured low micromolar affinity between full-length DKK1 and immobilized KRM1ECD (FigureΒ 2B). RESULTS |
|
173 177 DKK1 protein We confirm that the CRD2 of DKK1 is required and sufficient for binding to KRM1: In surface plasmon resonance (SPR), we measured low micromolar affinity between full-length DKK1 and immobilized KRM1ECD (FigureΒ 2B). RESULTS |
|
194 198 KRM1 protein We confirm that the CRD2 of DKK1 is required and sufficient for binding to KRM1: In surface plasmon resonance (SPR), we measured low micromolar affinity between full-length DKK1 and immobilized KRM1ECD (FigureΒ 2B). RESULTS |
|
198 201 ECD structure_element We confirm that the CRD2 of DKK1 is required and sufficient for binding to KRM1: In surface plasmon resonance (SPR), we measured low micromolar affinity between full-length DKK1 and immobilized KRM1ECD (FigureΒ 2B). RESULTS |
|
2 13 SUMO fusion experimental_method A SUMO fusion of DKK1L-CRD2 displayed a similar (slightly higher) affinity. RESULTS |
|
17 27 DKK1L-CRD2 structure_element A SUMO fusion of DKK1L-CRD2 displayed a similar (slightly higher) affinity. RESULTS |
|
66 74 affinity evidence A SUMO fusion of DKK1L-CRD2 displayed a similar (slightly higher) affinity. RESULTS |
|
15 26 SUMO fusion experimental_method In contrast, a SUMO fusion of DKK1CRD1-L did not display binding for concentrations tested up to 325Β ΞΌM (FigureΒ 2B). RESULTS |
|
30 40 DKK1CRD1-L structure_element In contrast, a SUMO fusion of DKK1CRD1-L did not display binding for concentrations tested up to 325Β ΞΌM (FigureΒ 2B). RESULTS |
|
13 32 DKK1-KRM1 interface site Overall, the DKK1-KRM1 interface is characterized by a large number of polar interactions but only few hydrophobic contacts (FigureΒ 2C). RESULTS |
|
71 89 polar interactions bond_interaction Overall, the DKK1-KRM1 interface is characterized by a large number of polar interactions but only few hydrophobic contacts (FigureΒ 2C). RESULTS |
|
103 123 hydrophobic contacts bond_interaction Overall, the DKK1-KRM1 interface is characterized by a large number of polar interactions but only few hydrophobic contacts (FigureΒ 2C). RESULTS |
|
4 21 crystal structure evidence The crystal structure gives an explanation for DKK1 loss-of-binding mutations identified previously: R191 of DKK1 forms a double salt bridge to D125 and E162 of KRM1 (FigureΒ 2C). RESULTS |
|
47 51 DKK1 protein The crystal structure gives an explanation for DKK1 loss-of-binding mutations identified previously: R191 of DKK1 forms a double salt bridge to D125 and E162 of KRM1 (FigureΒ 2C). RESULTS |
|
101 105 R191 residue_name_number The crystal structure gives an explanation for DKK1 loss-of-binding mutations identified previously: R191 of DKK1 forms a double salt bridge to D125 and E162 of KRM1 (FigureΒ 2C). RESULTS |
|
109 113 DKK1 protein The crystal structure gives an explanation for DKK1 loss-of-binding mutations identified previously: R191 of DKK1 forms a double salt bridge to D125 and E162 of KRM1 (FigureΒ 2C). RESULTS |
|
129 140 salt bridge bond_interaction The crystal structure gives an explanation for DKK1 loss-of-binding mutations identified previously: R191 of DKK1 forms a double salt bridge to D125 and E162 of KRM1 (FigureΒ 2C). RESULTS |
|
144 148 D125 residue_name_number The crystal structure gives an explanation for DKK1 loss-of-binding mutations identified previously: R191 of DKK1 forms a double salt bridge to D125 and E162 of KRM1 (FigureΒ 2C). RESULTS |
|
153 157 E162 residue_name_number The crystal structure gives an explanation for DKK1 loss-of-binding mutations identified previously: R191 of DKK1 forms a double salt bridge to D125 and E162 of KRM1 (FigureΒ 2C). RESULTS |
|
161 165 KRM1 protein The crystal structure gives an explanation for DKK1 loss-of-binding mutations identified previously: R191 of DKK1 forms a double salt bridge to D125 and E162 of KRM1 (FigureΒ 2C). RESULTS |
|
2 17 charge reversal experimental_method A charge reversal as in the mouse Dkk1 (mDkk1) R197E variant would severely disrupt the binding. RESULTS |
|
28 33 mouse taxonomy_domain A charge reversal as in the mouse Dkk1 (mDkk1) R197E variant would severely disrupt the binding. RESULTS |
|
34 38 Dkk1 protein A charge reversal as in the mouse Dkk1 (mDkk1) R197E variant would severely disrupt the binding. RESULTS |
|
40 45 mDkk1 protein A charge reversal as in the mouse Dkk1 (mDkk1) R197E variant would severely disrupt the binding. RESULTS |
|
47 52 R197E mutant A charge reversal as in the mouse Dkk1 (mDkk1) R197E variant would severely disrupt the binding. RESULTS |
|
15 19 K226 residue_name_number Similarly, the K226 side chain of DKK1, which points to a small hydrophobic pocket on the surface of KRM1 formed by Y108, W94, and W106, forms salt bridges with the side chains of KRM1 D88 and D90. RESULTS |
|
34 38 DKK1 protein Similarly, the K226 side chain of DKK1, which points to a small hydrophobic pocket on the surface of KRM1 formed by Y108, W94, and W106, forms salt bridges with the side chains of KRM1 D88 and D90. RESULTS |
|
64 82 hydrophobic pocket site Similarly, the K226 side chain of DKK1, which points to a small hydrophobic pocket on the surface of KRM1 formed by Y108, W94, and W106, forms salt bridges with the side chains of KRM1 D88 and D90. RESULTS |
|
101 105 KRM1 protein Similarly, the K226 side chain of DKK1, which points to a small hydrophobic pocket on the surface of KRM1 formed by Y108, W94, and W106, forms salt bridges with the side chains of KRM1 D88 and D90. RESULTS |
|
116 120 Y108 residue_name_number Similarly, the K226 side chain of DKK1, which points to a small hydrophobic pocket on the surface of KRM1 formed by Y108, W94, and W106, forms salt bridges with the side chains of KRM1 D88 and D90. RESULTS |
|
122 125 W94 residue_name_number Similarly, the K226 side chain of DKK1, which points to a small hydrophobic pocket on the surface of KRM1 formed by Y108, W94, and W106, forms salt bridges with the side chains of KRM1 D88 and D90. RESULTS |
|
131 135 W106 residue_name_number Similarly, the K226 side chain of DKK1, which points to a small hydrophobic pocket on the surface of KRM1 formed by Y108, W94, and W106, forms salt bridges with the side chains of KRM1 D88 and D90. RESULTS |
|
143 155 salt bridges bond_interaction Similarly, the K226 side chain of DKK1, which points to a small hydrophobic pocket on the surface of KRM1 formed by Y108, W94, and W106, forms salt bridges with the side chains of KRM1 D88 and D90. RESULTS |
|
180 184 KRM1 protein Similarly, the K226 side chain of DKK1, which points to a small hydrophobic pocket on the surface of KRM1 formed by Y108, W94, and W106, forms salt bridges with the side chains of KRM1 D88 and D90. RESULTS |
|
185 188 D88 residue_name_number Similarly, the K226 side chain of DKK1, which points to a small hydrophobic pocket on the surface of KRM1 formed by Y108, W94, and W106, forms salt bridges with the side chains of KRM1 D88 and D90. RESULTS |
|
193 196 D90 residue_name_number Similarly, the K226 side chain of DKK1, which points to a small hydrophobic pocket on the surface of KRM1 formed by Y108, W94, and W106, forms salt bridges with the side chains of KRM1 D88 and D90. RESULTS |
|
9 24 charge reversal experimental_method Again, a charge reversal as shown before for mDkk1 K232E would be incompatible with binding. RESULTS |
|
45 50 mDkk1 protein Again, a charge reversal as shown before for mDkk1 K232E would be incompatible with binding. RESULTS |
|
51 56 K232E mutant Again, a charge reversal as shown before for mDkk1 K232E would be incompatible with binding. RESULTS |
|
18 22 DKK1 protein The side chain of DKK1 S192 was also predicted to be involved in Krm binding. RESULTS |
|
23 27 S192 residue_name_number The side chain of DKK1 S192 was also predicted to be involved in Krm binding. RESULTS |
|
65 68 Krm protein_type The side chain of DKK1 S192 was also predicted to be involved in Krm binding. RESULTS |
|
52 56 D201 residue_name_number Indeed, we found (FigureΒ 2C) that the side chain of D201 of KRM1 forms two hydrogen bonds to the side-chain hydroxyl and the backbone amide of S192 (mouse, S198). RESULTS |
|
60 64 KRM1 protein Indeed, we found (FigureΒ 2C) that the side chain of D201 of KRM1 forms two hydrogen bonds to the side-chain hydroxyl and the backbone amide of S192 (mouse, S198). RESULTS |
|
75 89 hydrogen bonds bond_interaction Indeed, we found (FigureΒ 2C) that the side chain of D201 of KRM1 forms two hydrogen bonds to the side-chain hydroxyl and the backbone amide of S192 (mouse, S198). RESULTS |
|
143 147 S192 residue_name_number Indeed, we found (FigureΒ 2C) that the side chain of D201 of KRM1 forms two hydrogen bonds to the side-chain hydroxyl and the backbone amide of S192 (mouse, S198). RESULTS |
|
149 154 mouse taxonomy_domain Indeed, we found (FigureΒ 2C) that the side chain of D201 of KRM1 forms two hydrogen bonds to the side-chain hydroxyl and the backbone amide of S192 (mouse, S198). RESULTS |
|
156 160 S198 residue_name_number Indeed, we found (FigureΒ 2C) that the side chain of D201 of KRM1 forms two hydrogen bonds to the side-chain hydroxyl and the backbone amide of S192 (mouse, S198). RESULTS |
|
11 29 polar interactions bond_interaction Additional polar interactions are formed between the N140, S163, and Y165 side chains of KRM1 and DKK1 backbone carbonyls of W206, L190, and C189, respectively. RESULTS |
|
53 57 N140 residue_name_number Additional polar interactions are formed between the N140, S163, and Y165 side chains of KRM1 and DKK1 backbone carbonyls of W206, L190, and C189, respectively. RESULTS |
|
59 63 S163 residue_name_number Additional polar interactions are formed between the N140, S163, and Y165 side chains of KRM1 and DKK1 backbone carbonyls of W206, L190, and C189, respectively. RESULTS |
|
69 73 Y165 residue_name_number Additional polar interactions are formed between the N140, S163, and Y165 side chains of KRM1 and DKK1 backbone carbonyls of W206, L190, and C189, respectively. RESULTS |
|
89 93 KRM1 protein Additional polar interactions are formed between the N140, S163, and Y165 side chains of KRM1 and DKK1 backbone carbonyls of W206, L190, and C189, respectively. RESULTS |
|
98 102 DKK1 protein Additional polar interactions are formed between the N140, S163, and Y165 side chains of KRM1 and DKK1 backbone carbonyls of W206, L190, and C189, respectively. RESULTS |
|
125 129 W206 residue_name_number Additional polar interactions are formed between the N140, S163, and Y165 side chains of KRM1 and DKK1 backbone carbonyls of W206, L190, and C189, respectively. RESULTS |
|
131 135 L190 residue_name_number Additional polar interactions are formed between the N140, S163, and Y165 side chains of KRM1 and DKK1 backbone carbonyls of W206, L190, and C189, respectively. RESULTS |
|
141 145 C189 residue_name_number Additional polar interactions are formed between the N140, S163, and Y165 side chains of KRM1 and DKK1 backbone carbonyls of W206, L190, and C189, respectively. RESULTS |
|
16 20 DKK1 protein The carbonyl of DKK1 R224 is hydrogen bonded to Y105 and W106 of KRM1. RESULTS |
|
21 25 R224 residue_name_number The carbonyl of DKK1 R224 is hydrogen bonded to Y105 and W106 of KRM1. RESULTS |
|
29 44 hydrogen bonded bond_interaction The carbonyl of DKK1 R224 is hydrogen bonded to Y105 and W106 of KRM1. RESULTS |
|
48 52 Y105 residue_name_number The carbonyl of DKK1 R224 is hydrogen bonded to Y105 and W106 of KRM1. RESULTS |
|
57 61 W106 residue_name_number The carbonyl of DKK1 R224 is hydrogen bonded to Y105 and W106 of KRM1. RESULTS |
|
65 69 KRM1 protein The carbonyl of DKK1 R224 is hydrogen bonded to Y105 and W106 of KRM1. RESULTS |
|
20 23 Dkk protein_type We suspect that the Dkk charge reversal mutations performed in the murine background and shown toΒ diminish Krm binding K211E and R203E (mouse K217E andΒ R209E) do so likely indirectly by disruptionΒ of the Dkk fold. RESULTS |
|
24 49 charge reversal mutations experimental_method We suspect that the Dkk charge reversal mutations performed in the murine background and shown toΒ diminish Krm binding K211E and R203E (mouse K217E andΒ R209E) do so likely indirectly by disruptionΒ of the Dkk fold. RESULTS |
|
67 73 murine taxonomy_domain We suspect that the Dkk charge reversal mutations performed in the murine background and shown toΒ diminish Krm binding K211E and R203E (mouse K217E andΒ R209E) do so likely indirectly by disruptionΒ of the Dkk fold. RESULTS |
|
107 110 Krm protein_type We suspect that the Dkk charge reversal mutations performed in the murine background and shown toΒ diminish Krm binding K211E and R203E (mouse K217E andΒ R209E) do so likely indirectly by disruptionΒ of the Dkk fold. RESULTS |
|
119 124 K211E mutant We suspect that the Dkk charge reversal mutations performed in the murine background and shown toΒ diminish Krm binding K211E and R203E (mouse K217E andΒ R209E) do so likely indirectly by disruptionΒ of the Dkk fold. RESULTS |
|
129 134 R203E mutant We suspect that the Dkk charge reversal mutations performed in the murine background and shown toΒ diminish Krm binding K211E and R203E (mouse K217E andΒ R209E) do so likely indirectly by disruptionΒ of the Dkk fold. RESULTS |
|
136 141 mouse taxonomy_domain We suspect that the Dkk charge reversal mutations performed in the murine background and shown toΒ diminish Krm binding K211E and R203E (mouse K217E andΒ R209E) do so likely indirectly by disruptionΒ of the Dkk fold. RESULTS |
|
142 147 K217E mutant We suspect that the Dkk charge reversal mutations performed in the murine background and shown toΒ diminish Krm binding K211E and R203E (mouse K217E andΒ R209E) do so likely indirectly by disruptionΒ of the Dkk fold. RESULTS |
|
152 157 R209E mutant We suspect that the Dkk charge reversal mutations performed in the murine background and shown toΒ diminish Krm binding K211E and R203E (mouse K217E andΒ R209E) do so likely indirectly by disruptionΒ of the Dkk fold. RESULTS |
|
204 207 Dkk protein_type We suspect that the Dkk charge reversal mutations performed in the murine background and shown toΒ diminish Krm binding K211E and R203E (mouse K217E andΒ R209E) do so likely indirectly by disruptionΒ of the Dkk fold. RESULTS |
|
25 42 DKK1 binding site site We further validated the DKK1 binding siteΒ onΒ KRM1 by introducing glycosylation sites at the KR (90DVS92βNVS) and WSC (189VCF191βNCS) domains pointing toward DKK (Figures 2A and 2D). RESULTS |
|
46 50 KRM1 protein We further validated the DKK1 binding siteΒ onΒ KRM1 by introducing glycosylation sites at the KR (90DVS92βNVS) and WSC (189VCF191βNCS) domains pointing toward DKK (Figures 2A and 2D). RESULTS |
|
54 65 introducing experimental_method We further validated the DKK1 binding siteΒ onΒ KRM1 by introducing glycosylation sites at the KR (90DVS92βNVS) and WSC (189VCF191βNCS) domains pointing toward DKK (Figures 2A and 2D). RESULTS |
|
66 85 glycosylation sites site We further validated the DKK1 binding siteΒ onΒ KRM1 by introducing glycosylation sites at the KR (90DVS92βNVS) and WSC (189VCF191βNCS) domains pointing toward DKK (Figures 2A and 2D). RESULTS |
|
93 95 KR structure_element We further validated the DKK1 binding siteΒ onΒ KRM1 by introducing glycosylation sites at the KR (90DVS92βNVS) and WSC (189VCF191βNCS) domains pointing toward DKK (Figures 2A and 2D). RESULTS |
|
97 108 90DVS92βNVS mutant We further validated the DKK1 binding siteΒ onΒ KRM1 by introducing glycosylation sites at the KR (90DVS92βNVS) and WSC (189VCF191βNCS) domains pointing toward DKK (Figures 2A and 2D). RESULTS |
|
114 117 WSC structure_element We further validated the DKK1 binding siteΒ onΒ KRM1 by introducing glycosylation sites at the KR (90DVS92βNVS) and WSC (189VCF191βNCS) domains pointing toward DKK (Figures 2A and 2D). RESULTS |
|
119 132 189VCF191βNCS mutant We further validated the DKK1 binding siteΒ onΒ KRM1 by introducing glycosylation sites at the KR (90DVS92βNVS) and WSC (189VCF191βNCS) domains pointing toward DKK (Figures 2A and 2D). RESULTS |
|
158 161 DKK protein We further validated the DKK1 binding siteΒ onΒ KRM1 by introducing glycosylation sites at the KR (90DVS92βNVS) and WSC (189VCF191βNCS) domains pointing toward DKK (Figures 2A and 2D). RESULTS |
|
16 32 N-linked glycans ptm Introduction of N-linked glycans in protein-protein-binding sites is an established way of disrupting protein-binding interfaces. RESULTS |
|
36 65 protein-protein-binding sites site Introduction of N-linked glycans in protein-protein-binding sites is an established way of disrupting protein-binding interfaces. RESULTS |
|
102 128 protein-binding interfaces site Introduction of N-linked glycans in protein-protein-binding sites is an established way of disrupting protein-binding interfaces. RESULTS |
|
5 15 ectodomain structure_element Both ectodomain mutants were secreted comparably with the wild-type, indicating correct folding, but failed to achieve any detectable binding in SPR using full-length DKK1 as analyte. RESULTS |
|
16 23 mutants protein_state Both ectodomain mutants were secreted comparably with the wild-type, indicating correct folding, but failed to achieve any detectable binding in SPR using full-length DKK1 as analyte. RESULTS |
|
58 67 wild-type protein_state Both ectodomain mutants were secreted comparably with the wild-type, indicating correct folding, but failed to achieve any detectable binding in SPR using full-length DKK1 as analyte. RESULTS |
|
145 148 SPR experimental_method Both ectodomain mutants were secreted comparably with the wild-type, indicating correct folding, but failed to achieve any detectable binding in SPR using full-length DKK1 as analyte. RESULTS |
|
155 166 full-length protein_state Both ectodomain mutants were secreted comparably with the wild-type, indicating correct folding, but failed to achieve any detectable binding in SPR using full-length DKK1 as analyte. RESULTS |
|
167 171 DKK1 protein Both ectodomain mutants were secreted comparably with the wild-type, indicating correct folding, but failed to achieve any detectable binding in SPR using full-length DKK1 as analyte. RESULTS |
|
15 21 mutant protein_state In contrast, a mutant carrying an additional N-glycan outside the interface at the CUB domain (309NQA311βNQS), was wild-type-like in DKK1 binding (FigureΒ 2D). RESULTS |
|
45 53 N-glycan ptm In contrast, a mutant carrying an additional N-glycan outside the interface at the CUB domain (309NQA311βNQS), was wild-type-like in DKK1 binding (FigureΒ 2D). RESULTS |
|
66 75 interface site In contrast, a mutant carrying an additional N-glycan outside the interface at the CUB domain (309NQA311βNQS), was wild-type-like in DKK1 binding (FigureΒ 2D). RESULTS |
|
83 86 CUB structure_element In contrast, a mutant carrying an additional N-glycan outside the interface at the CUB domain (309NQA311βNQS), was wild-type-like in DKK1 binding (FigureΒ 2D). RESULTS |
|
95 108 309NQA311βNQS mutant In contrast, a mutant carrying an additional N-glycan outside the interface at the CUB domain (309NQA311βNQS), was wild-type-like in DKK1 binding (FigureΒ 2D). RESULTS |
|
115 124 wild-type protein_state In contrast, a mutant carrying an additional N-glycan outside the interface at the CUB domain (309NQA311βNQS), was wild-type-like in DKK1 binding (FigureΒ 2D). RESULTS |
|
133 137 DKK1 protein In contrast, a mutant carrying an additional N-glycan outside the interface at the CUB domain (309NQA311βNQS), was wild-type-like in DKK1 binding (FigureΒ 2D). RESULTS |
|
27 49 LRP6-KRM1 Binding Site site Identification of a Direct LRP6-KRM1 Binding Site RESULTS |
|
4 31 LRP6PE3PE4-DKK1CRD2-KRM1ECD complex_assembly The LRP6PE3PE4-DKK1CRD2-KRM1ECD complex structure reveals no direct interactions between KRM1 and LRP6. RESULTS |
|
40 49 structure evidence The LRP6PE3PE4-DKK1CRD2-KRM1ECD complex structure reveals no direct interactions between KRM1 and LRP6. RESULTS |
|
89 93 KRM1 protein The LRP6PE3PE4-DKK1CRD2-KRM1ECD complex structure reveals no direct interactions between KRM1 and LRP6. RESULTS |
|
98 102 LRP6 protein The LRP6PE3PE4-DKK1CRD2-KRM1ECD complex structure reveals no direct interactions between KRM1 and LRP6. RESULTS |
|
35 47 complex with protein_state We constructed inΒ silico a ternary complex with a close to full-length LRP6 ectodomain (PE1PE2PE3PE4 horse shoe) similar to but without refinement against electron microscopy (EM) or small-angle X-ray scattering data. RESULTS |
|
59 70 full-length protein_state We constructed inΒ silico a ternary complex with a close to full-length LRP6 ectodomain (PE1PE2PE3PE4 horse shoe) similar to but without refinement against electron microscopy (EM) or small-angle X-ray scattering data. RESULTS |
|
71 75 LRP6 protein We constructed inΒ silico a ternary complex with a close to full-length LRP6 ectodomain (PE1PE2PE3PE4 horse shoe) similar to but without refinement against electron microscopy (EM) or small-angle X-ray scattering data. RESULTS |
|
76 86 ectodomain structure_element We constructed inΒ silico a ternary complex with a close to full-length LRP6 ectodomain (PE1PE2PE3PE4 horse shoe) similar to but without refinement against electron microscopy (EM) or small-angle X-ray scattering data. RESULTS |
|
88 100 PE1PE2PE3PE4 structure_element We constructed inΒ silico a ternary complex with a close to full-length LRP6 ectodomain (PE1PE2PE3PE4 horse shoe) similar to but without refinement against electron microscopy (EM) or small-angle X-ray scattering data. RESULTS |
|
101 111 horse shoe structure_element We constructed inΒ silico a ternary complex with a close to full-length LRP6 ectodomain (PE1PE2PE3PE4 horse shoe) similar to but without refinement against electron microscopy (EM) or small-angle X-ray scattering data. RESULTS |
|
155 174 electron microscopy experimental_method We constructed inΒ silico a ternary complex with a close to full-length LRP6 ectodomain (PE1PE2PE3PE4 horse shoe) similar to but without refinement against electron microscopy (EM) or small-angle X-ray scattering data. RESULTS |
|
176 178 EM experimental_method We constructed inΒ silico a ternary complex with a close to full-length LRP6 ectodomain (PE1PE2PE3PE4 horse shoe) similar to but without refinement against electron microscopy (EM) or small-angle X-ray scattering data. RESULTS |
|
183 211 small-angle X-ray scattering experimental_method We constructed inΒ silico a ternary complex with a close to full-length LRP6 ectodomain (PE1PE2PE3PE4 horse shoe) similar to but without refinement against electron microscopy (EM) or small-angle X-ray scattering data. RESULTS |
|
13 19 PE3PE4 structure_element An auxiliary PE3PE4 fragment was superimposed via PE4 onto PE3 of the crystal structure, and the LRP6PE1PE2 structure was superimposed via PE2 onto PE3 of this auxiliary fragment (FigureΒ 3A). RESULTS |
|
33 45 superimposed experimental_method An auxiliary PE3PE4 fragment was superimposed via PE4 onto PE3 of the crystal structure, and the LRP6PE1PE2 structure was superimposed via PE2 onto PE3 of this auxiliary fragment (FigureΒ 3A). RESULTS |
|
50 53 PE4 structure_element An auxiliary PE3PE4 fragment was superimposed via PE4 onto PE3 of the crystal structure, and the LRP6PE1PE2 structure was superimposed via PE2 onto PE3 of this auxiliary fragment (FigureΒ 3A). RESULTS |
|
59 62 PE3 structure_element An auxiliary PE3PE4 fragment was superimposed via PE4 onto PE3 of the crystal structure, and the LRP6PE1PE2 structure was superimposed via PE2 onto PE3 of this auxiliary fragment (FigureΒ 3A). RESULTS |
|
70 87 crystal structure evidence An auxiliary PE3PE4 fragment was superimposed via PE4 onto PE3 of the crystal structure, and the LRP6PE1PE2 structure was superimposed via PE2 onto PE3 of this auxiliary fragment (FigureΒ 3A). RESULTS |
|
97 101 LRP6 protein An auxiliary PE3PE4 fragment was superimposed via PE4 onto PE3 of the crystal structure, and the LRP6PE1PE2 structure was superimposed via PE2 onto PE3 of this auxiliary fragment (FigureΒ 3A). RESULTS |
|
101 107 PE1PE2 structure_element An auxiliary PE3PE4 fragment was superimposed via PE4 onto PE3 of the crystal structure, and the LRP6PE1PE2 structure was superimposed via PE2 onto PE3 of this auxiliary fragment (FigureΒ 3A). RESULTS |
|
108 117 structure evidence An auxiliary PE3PE4 fragment was superimposed via PE4 onto PE3 of the crystal structure, and the LRP6PE1PE2 structure was superimposed via PE2 onto PE3 of this auxiliary fragment (FigureΒ 3A). RESULTS |
|
122 134 superimposed experimental_method An auxiliary PE3PE4 fragment was superimposed via PE4 onto PE3 of the crystal structure, and the LRP6PE1PE2 structure was superimposed via PE2 onto PE3 of this auxiliary fragment (FigureΒ 3A). RESULTS |
|
139 142 PE2 structure_element An auxiliary PE3PE4 fragment was superimposed via PE4 onto PE3 of the crystal structure, and the LRP6PE1PE2 structure was superimposed via PE2 onto PE3 of this auxiliary fragment (FigureΒ 3A). RESULTS |
|
148 151 PE3 structure_element An auxiliary PE3PE4 fragment was superimposed via PE4 onto PE3 of the crystal structure, and the LRP6PE1PE2 structure was superimposed via PE2 onto PE3 of this auxiliary fragment (FigureΒ 3A). RESULTS |
|
98 117 Ca2+-binding region site For this crude approximation of a true ternary complex, we noted very close proximity between the Ca2+-binding region of KRM1 and the top face of the PE2 Ξ² propeller of LRP6. RESULTS |
|
121 125 KRM1 protein For this crude approximation of a true ternary complex, we noted very close proximity between the Ca2+-binding region of KRM1 and the top face of the PE2 Ξ² propeller of LRP6. RESULTS |
|
150 153 PE2 structure_element For this crude approximation of a true ternary complex, we noted very close proximity between the Ca2+-binding region of KRM1 and the top face of the PE2 Ξ² propeller of LRP6. RESULTS |
|
154 165 Ξ² propeller structure_element For this crude approximation of a true ternary complex, we noted very close proximity between the Ca2+-binding region of KRM1 and the top face of the PE2 Ξ² propeller of LRP6. RESULTS |
|
169 173 LRP6 protein For this crude approximation of a true ternary complex, we noted very close proximity between the Ca2+-binding region of KRM1 and the top face of the PE2 Ξ² propeller of LRP6. RESULTS |
|
4 19 solvent-exposed protein_state The solvent-exposed residues R307, I308, and N309 of the central Ca2+-binding Ξ² connection loop of KRM1 would be almost ideally positioned for binding to this face, which is commonly used as a binding site on Ξ² propellers. RESULTS |
|
29 33 R307 residue_name_number The solvent-exposed residues R307, I308, and N309 of the central Ca2+-binding Ξ² connection loop of KRM1 would be almost ideally positioned for binding to this face, which is commonly used as a binding site on Ξ² propellers. RESULTS |
|
35 39 I308 residue_name_number The solvent-exposed residues R307, I308, and N309 of the central Ca2+-binding Ξ² connection loop of KRM1 would be almost ideally positioned for binding to this face, which is commonly used as a binding site on Ξ² propellers. RESULTS |
|
45 49 N309 residue_name_number The solvent-exposed residues R307, I308, and N309 of the central Ca2+-binding Ξ² connection loop of KRM1 would be almost ideally positioned for binding to this face, which is commonly used as a binding site on Ξ² propellers. RESULTS |
|
65 95 Ca2+-binding Ξ² connection loop structure_element The solvent-exposed residues R307, I308, and N309 of the central Ca2+-binding Ξ² connection loop of KRM1 would be almost ideally positioned for binding to this face, which is commonly used as a binding site on Ξ² propellers. RESULTS |
|
99 103 KRM1 protein The solvent-exposed residues R307, I308, and N309 of the central Ca2+-binding Ξ² connection loop of KRM1 would be almost ideally positioned for binding to this face, which is commonly used as a binding site on Ξ² propellers. RESULTS |
|
193 205 binding site site The solvent-exposed residues R307, I308, and N309 of the central Ca2+-binding Ξ² connection loop of KRM1 would be almost ideally positioned for binding to this face, which is commonly used as a binding site on Ξ² propellers. RESULTS |
|
209 221 Ξ² propellers structure_element The solvent-exposed residues R307, I308, and N309 of the central Ca2+-binding Ξ² connection loop of KRM1 would be almost ideally positioned for binding to this face, which is commonly used as a binding site on Ξ² propellers. RESULTS |
|
20 28 arginine residue_name Peptides containing arginine/lysine, isoleucine, and asparagine (consensus sequence N-X-I-(G)-R/K) are also employed by DKK1 and SOST to bind to LRP6 (albeit to propeller 1 |
|
29 35 lysine residue_name Peptides containing arginine/lysine, isoleucine, and asparagine (consensus sequence N-X-I-(G)-R/K) are also employed by DKK1 and SOST to bind to LRP6 (albeit to propeller 1 |
|
37 47 isoleucine residue_name Peptides containing arginine/lysine, isoleucine, and asparagine (consensus sequence N-X-I-(G)-R/K) are also employed by DKK1 and SOST to bind to LRP6 (albeit to propeller 1 |
|
53 63 asparagine residue_name Peptides containing arginine/lysine, isoleucine, and asparagine (consensus sequence N-X-I-(G)-R/K) are also employed by DKK1 and SOST to bind to LRP6 (albeit to propeller 1 |
|
84 97 N-X-I-(G)-R/K structure_element Peptides containing arginine/lysine, isoleucine, and asparagine (consensus sequence N-X-I-(G)-R/K) are also employed by DKK1 and SOST to bind to LRP6 (albeit to propeller 1 |
|
120 124 DKK1 protein Peptides containing arginine/lysine, isoleucine, and asparagine (consensus sequence N-X-I-(G)-R/K) are also employed by DKK1 and SOST to bind to LRP6 (albeit to propeller 1 |
|
129 133 SOST protein Peptides containing arginine/lysine, isoleucine, and asparagine (consensus sequence N-X-I-(G)-R/K) are also employed by DKK1 and SOST to bind to LRP6 (albeit to propeller 1 |
|
145 149 LRP6 protein Peptides containing arginine/lysine, isoleucine, and asparagine (consensus sequence N-X-I-(G)-R/K) are also employed by DKK1 and SOST to bind to LRP6 (albeit to propeller 1 |
|
161 172 propeller 1 structure_element Peptides containing arginine/lysine, isoleucine, and asparagine (consensus sequence N-X-I-(G)-R/K) are also employed by DKK1 and SOST to bind to LRP6 (albeit to propeller 1 |
|
31 35 KRM1 protein To support the hypothesis that KRM1CUB binds to LRP6PE2, we used SPR and compared binding of the wild-type and the GlycoCUB mutant of KRM1ECD (bearing an N-glycosylation site at N309) with a purified LRP6PE1PE2 fragment. RESULTS |
|
35 38 CUB structure_element To support the hypothesis that KRM1CUB binds to LRP6PE2, we used SPR and compared binding of the wild-type and the GlycoCUB mutant of KRM1ECD (bearing an N-glycosylation site at N309) with a purified LRP6PE1PE2 fragment. RESULTS |
|
39 47 binds to protein_state To support the hypothesis that KRM1CUB binds to LRP6PE2, we used SPR and compared binding of the wild-type and the GlycoCUB mutant of KRM1ECD (bearing an N-glycosylation site at N309) with a purified LRP6PE1PE2 fragment. RESULTS |
|
48 52 LRP6 protein To support the hypothesis that KRM1CUB binds to LRP6PE2, we used SPR and compared binding of the wild-type and the GlycoCUB mutant of KRM1ECD (bearing an N-glycosylation site at N309) with a purified LRP6PE1PE2 fragment. RESULTS |
|
52 55 PE2 structure_element To support the hypothesis that KRM1CUB binds to LRP6PE2, we used SPR and compared binding of the wild-type and the GlycoCUB mutant of KRM1ECD (bearing an N-glycosylation site at N309) with a purified LRP6PE1PE2 fragment. RESULTS |
|
65 68 SPR experimental_method To support the hypothesis that KRM1CUB binds to LRP6PE2, we used SPR and compared binding of the wild-type and the GlycoCUB mutant of KRM1ECD (bearing an N-glycosylation site at N309) with a purified LRP6PE1PE2 fragment. RESULTS |
|
97 106 wild-type protein_state To support the hypothesis that KRM1CUB binds to LRP6PE2, we used SPR and compared binding of the wild-type and the GlycoCUB mutant of KRM1ECD (bearing an N-glycosylation site at N309) with a purified LRP6PE1PE2 fragment. RESULTS |
|
115 130 GlycoCUB mutant protein_state To support the hypothesis that KRM1CUB binds to LRP6PE2, we used SPR and compared binding of the wild-type and the GlycoCUB mutant of KRM1ECD (bearing an N-glycosylation site at N309) with a purified LRP6PE1PE2 fragment. RESULTS |
|
134 138 KRM1 protein To support the hypothesis that KRM1CUB binds to LRP6PE2, we used SPR and compared binding of the wild-type and the GlycoCUB mutant of KRM1ECD (bearing an N-glycosylation site at N309) with a purified LRP6PE1PE2 fragment. RESULTS |
|
138 141 ECD structure_element To support the hypothesis that KRM1CUB binds to LRP6PE2, we used SPR and compared binding of the wild-type and the GlycoCUB mutant of KRM1ECD (bearing an N-glycosylation site at N309) with a purified LRP6PE1PE2 fragment. RESULTS |
|
154 174 N-glycosylation site site To support the hypothesis that KRM1CUB binds to LRP6PE2, we used SPR and compared binding of the wild-type and the GlycoCUB mutant of KRM1ECD (bearing an N-glycosylation site at N309) with a purified LRP6PE1PE2 fragment. RESULTS |
|
178 182 N309 residue_name_number To support the hypothesis that KRM1CUB binds to LRP6PE2, we used SPR and compared binding of the wild-type and the GlycoCUB mutant of KRM1ECD (bearing an N-glycosylation site at N309) with a purified LRP6PE1PE2 fragment. RESULTS |
|
200 204 LRP6 protein To support the hypothesis that KRM1CUB binds to LRP6PE2, we used SPR and compared binding of the wild-type and the GlycoCUB mutant of KRM1ECD (bearing an N-glycosylation site at N309) with a purified LRP6PE1PE2 fragment. RESULTS |
|
204 210 PE1PE2 structure_element To support the hypothesis that KRM1CUB binds to LRP6PE2, we used SPR and compared binding of the wild-type and the GlycoCUB mutant of KRM1ECD (bearing an N-glycosylation site at N309) with a purified LRP6PE1PE2 fragment. RESULTS |
|
29 39 absence of protein_state Indeed, we found that in the absence of Dkk, KRM1ECD bound with considerable affinity to LRP6PE1PE2 (FigureΒ 3C). RESULTS |
|
40 43 Dkk protein_type Indeed, we found that in the absence of Dkk, KRM1ECD bound with considerable affinity to LRP6PE1PE2 (FigureΒ 3C). RESULTS |
|
45 49 KRM1 protein Indeed, we found that in the absence of Dkk, KRM1ECD bound with considerable affinity to LRP6PE1PE2 (FigureΒ 3C). RESULTS |
|
49 52 ECD structure_element Indeed, we found that in the absence of Dkk, KRM1ECD bound with considerable affinity to LRP6PE1PE2 (FigureΒ 3C). RESULTS |
|
53 58 bound protein_state Indeed, we found that in the absence of Dkk, KRM1ECD bound with considerable affinity to LRP6PE1PE2 (FigureΒ 3C). RESULTS |
|
86 88 to protein_state Indeed, we found that in the absence of Dkk, KRM1ECD bound with considerable affinity to LRP6PE1PE2 (FigureΒ 3C). RESULTS |
|
89 93 LRP6 protein Indeed, we found that in the absence of Dkk, KRM1ECD bound with considerable affinity to LRP6PE1PE2 (FigureΒ 3C). RESULTS |
|
93 99 PE1PE2 structure_element Indeed, we found that in the absence of Dkk, KRM1ECD bound with considerable affinity to LRP6PE1PE2 (FigureΒ 3C). RESULTS |
|
55 59 KRM1 protein In contrast, no saturable binding was observed between KRM1 and LRP6PE3PE4. RESULTS |
|
64 68 LRP6 protein In contrast, no saturable binding was observed between KRM1 and LRP6PE3PE4. RESULTS |
|
68 74 PE3PE4 structure_element In contrast, no saturable binding was observed between KRM1 and LRP6PE3PE4. RESULTS |
|
0 15 Introduction of experimental_method Introduction of an N-glycosylation site at N309 in KRM1ECD abolished LRP6PE1PE2 binding (FigureΒ 3C), while binding to DKK1 was unaffected (FigureΒ 2D). RESULTS |
|
19 39 N-glycosylation site site Introduction of an N-glycosylation site at N309 in KRM1ECD abolished LRP6PE1PE2 binding (FigureΒ 3C), while binding to DKK1 was unaffected (FigureΒ 2D). RESULTS |
|
43 47 N309 residue_name_number Introduction of an N-glycosylation site at N309 in KRM1ECD abolished LRP6PE1PE2 binding (FigureΒ 3C), while binding to DKK1 was unaffected (FigureΒ 2D). RESULTS |
|
51 55 KRM1 protein Introduction of an N-glycosylation site at N309 in KRM1ECD abolished LRP6PE1PE2 binding (FigureΒ 3C), while binding to DKK1 was unaffected (FigureΒ 2D). RESULTS |
|
55 58 ECD structure_element Introduction of an N-glycosylation site at N309 in KRM1ECD abolished LRP6PE1PE2 binding (FigureΒ 3C), while binding to DKK1 was unaffected (FigureΒ 2D). RESULTS |
|
69 73 LRP6 protein Introduction of an N-glycosylation site at N309 in KRM1ECD abolished LRP6PE1PE2 binding (FigureΒ 3C), while binding to DKK1 was unaffected (FigureΒ 2D). RESULTS |
|
73 79 PE1PE2 structure_element Introduction of an N-glycosylation site at N309 in KRM1ECD abolished LRP6PE1PE2 binding (FigureΒ 3C), while binding to DKK1 was unaffected (FigureΒ 2D). RESULTS |
|
118 122 DKK1 protein Introduction of an N-glycosylation site at N309 in KRM1ECD abolished LRP6PE1PE2 binding (FigureΒ 3C), while binding to DKK1 was unaffected (FigureΒ 2D). RESULTS |
|
31 43 binding site site We conclude that the predicted binding site between KRM1CUB and LRP6PE2 is a strong candidate for mediating the direct Lrp6-Krm interaction, which is thought to increase Wnt responsiveness by stabilizing Lrp6 at the cell surface. RESULTS |
|
52 56 KRM1 protein We conclude that the predicted binding site between KRM1CUB and LRP6PE2 is a strong candidate for mediating the direct Lrp6-Krm interaction, which is thought to increase Wnt responsiveness by stabilizing Lrp6 at the cell surface. RESULTS |
|
56 59 CUB structure_element We conclude that the predicted binding site between KRM1CUB and LRP6PE2 is a strong candidate for mediating the direct Lrp6-Krm interaction, which is thought to increase Wnt responsiveness by stabilizing Lrp6 at the cell surface. RESULTS |
|
64 68 LRP6 protein We conclude that the predicted binding site between KRM1CUB and LRP6PE2 is a strong candidate for mediating the direct Lrp6-Krm interaction, which is thought to increase Wnt responsiveness by stabilizing Lrp6 at the cell surface. RESULTS |
|
68 71 PE2 structure_element We conclude that the predicted binding site between KRM1CUB and LRP6PE2 is a strong candidate for mediating the direct Lrp6-Krm interaction, which is thought to increase Wnt responsiveness by stabilizing Lrp6 at the cell surface. RESULTS |
|
119 127 Lrp6-Krm complex_assembly We conclude that the predicted binding site between KRM1CUB and LRP6PE2 is a strong candidate for mediating the direct Lrp6-Krm interaction, which is thought to increase Wnt responsiveness by stabilizing Lrp6 at the cell surface. RESULTS |
|
170 173 Wnt protein_type We conclude that the predicted binding site between KRM1CUB and LRP6PE2 is a strong candidate for mediating the direct Lrp6-Krm interaction, which is thought to increase Wnt responsiveness by stabilizing Lrp6 at the cell surface. RESULTS |
|
204 208 Lrp6 protein We conclude that the predicted binding site between KRM1CUB and LRP6PE2 is a strong candidate for mediating the direct Lrp6-Krm interaction, which is thought to increase Wnt responsiveness by stabilizing Lrp6 at the cell surface. RESULTS |
|
55 67 binding site site Further experiments are required to pinpoint the exact binding site. RESULTS |
|
9 13 LRP6 protein Although LRP6PE1 appears somewhat out of reach in the modeled ternary complex, it cannot be excluded as the Krm binding site in the ternary complex and LRP6-Krm binary complex. RESULTS |
|
13 16 PE1 structure_element Although LRP6PE1 appears somewhat out of reach in the modeled ternary complex, it cannot be excluded as the Krm binding site in the ternary complex and LRP6-Krm binary complex. RESULTS |
|
108 124 Krm binding site site Although LRP6PE1 appears somewhat out of reach in the modeled ternary complex, it cannot be excluded as the Krm binding site in the ternary complex and LRP6-Krm binary complex. RESULTS |
|
152 160 LRP6-Krm complex_assembly Although LRP6PE1 appears somewhat out of reach in the modeled ternary complex, it cannot be excluded as the Krm binding site in the ternary complex and LRP6-Krm binary complex. RESULTS |
|
4 15 presence of protein_state The presence of DKK may govern which propeller (PE1 versus PE2) of LRP6 is available for Krm binding. RESULTS |
|
16 19 DKK protein The presence of DKK may govern which propeller (PE1 versus PE2) of LRP6 is available for Krm binding. RESULTS |
|
37 46 propeller structure_element The presence of DKK may govern which propeller (PE1 versus PE2) of LRP6 is available for Krm binding. RESULTS |
|
48 51 PE1 structure_element The presence of DKK may govern which propeller (PE1 versus PE2) of LRP6 is available for Krm binding. RESULTS |
|
59 62 PE2 structure_element The presence of DKK may govern which propeller (PE1 versus PE2) of LRP6 is available for Krm binding. RESULTS |
|
67 71 LRP6 protein The presence of DKK may govern which propeller (PE1 versus PE2) of LRP6 is available for Krm binding. RESULTS |
|
89 92 Krm protein_type The presence of DKK may govern which propeller (PE1 versus PE2) of LRP6 is available for Krm binding. RESULTS |
|
37 62 KRM1CUB-LRP6PE2 interface site Apparent binding across the proposed KRM1CUB-LRP6PE2 interface is expected to be higher once Krm is also cross-linked to LRP6PE3 via DKK1CRD2 (FigureΒ 3D). RESULTS |
|
93 96 Krm protein_type Apparent binding across the proposed KRM1CUB-LRP6PE2 interface is expected to be higher once Krm is also cross-linked to LRP6PE3 via DKK1CRD2 (FigureΒ 3D). RESULTS |
|
121 125 LRP6 protein Apparent binding across the proposed KRM1CUB-LRP6PE2 interface is expected to be higher once Krm is also cross-linked to LRP6PE3 via DKK1CRD2 (FigureΒ 3D). RESULTS |
|
125 128 PE3 structure_element Apparent binding across the proposed KRM1CUB-LRP6PE2 interface is expected to be higher once Krm is also cross-linked to LRP6PE3 via DKK1CRD2 (FigureΒ 3D). RESULTS |
|
133 137 DKK1 protein Apparent binding across the proposed KRM1CUB-LRP6PE2 interface is expected to be higher once Krm is also cross-linked to LRP6PE3 via DKK1CRD2 (FigureΒ 3D). RESULTS |
|
137 141 CRD2 structure_element Apparent binding across the proposed KRM1CUB-LRP6PE2 interface is expected to be higher once Krm is also cross-linked to LRP6PE3 via DKK1CRD2 (FigureΒ 3D). RESULTS |
|
15 32 negative-stain EM experimental_method Low-resolution negative-stain EM and small-angle X-ray scattering studies of LRP6PE1PE2PE3PE4, in isolation and in complex with Dkk1, plus negative-stain EM of full-length LRP6 ectodomain, have indicated curved, platform-like conformations but also potential flexibility between PE2 and PE3. RESULTS |
|
37 65 small-angle X-ray scattering experimental_method Low-resolution negative-stain EM and small-angle X-ray scattering studies of LRP6PE1PE2PE3PE4, in isolation and in complex with Dkk1, plus negative-stain EM of full-length LRP6 ectodomain, have indicated curved, platform-like conformations but also potential flexibility between PE2 and PE3. RESULTS |
|
77 81 LRP6 protein Low-resolution negative-stain EM and small-angle X-ray scattering studies of LRP6PE1PE2PE3PE4, in isolation and in complex with Dkk1, plus negative-stain EM of full-length LRP6 ectodomain, have indicated curved, platform-like conformations but also potential flexibility between PE2 and PE3. RESULTS |
|
81 93 PE1PE2PE3PE4 structure_element Low-resolution negative-stain EM and small-angle X-ray scattering studies of LRP6PE1PE2PE3PE4, in isolation and in complex with Dkk1, plus negative-stain EM of full-length LRP6 ectodomain, have indicated curved, platform-like conformations but also potential flexibility between PE2 and PE3. RESULTS |
|
95 107 in isolation protein_state Low-resolution negative-stain EM and small-angle X-ray scattering studies of LRP6PE1PE2PE3PE4, in isolation and in complex with Dkk1, plus negative-stain EM of full-length LRP6 ectodomain, have indicated curved, platform-like conformations but also potential flexibility between PE2 and PE3. RESULTS |
|
112 127 in complex with protein_state Low-resolution negative-stain EM and small-angle X-ray scattering studies of LRP6PE1PE2PE3PE4, in isolation and in complex with Dkk1, plus negative-stain EM of full-length LRP6 ectodomain, have indicated curved, platform-like conformations but also potential flexibility between PE2 and PE3. RESULTS |
|
128 132 Dkk1 protein_type Low-resolution negative-stain EM and small-angle X-ray scattering studies of LRP6PE1PE2PE3PE4, in isolation and in complex with Dkk1, plus negative-stain EM of full-length LRP6 ectodomain, have indicated curved, platform-like conformations but also potential flexibility between PE2 and PE3. RESULTS |
|
139 156 negative-stain EM experimental_method Low-resolution negative-stain EM and small-angle X-ray scattering studies of LRP6PE1PE2PE3PE4, in isolation and in complex with Dkk1, plus negative-stain EM of full-length LRP6 ectodomain, have indicated curved, platform-like conformations but also potential flexibility between PE2 and PE3. RESULTS |
|
160 171 full-length protein_state Low-resolution negative-stain EM and small-angle X-ray scattering studies of LRP6PE1PE2PE3PE4, in isolation and in complex with Dkk1, plus negative-stain EM of full-length LRP6 ectodomain, have indicated curved, platform-like conformations but also potential flexibility between PE2 and PE3. RESULTS |
|
172 176 LRP6 protein Low-resolution negative-stain EM and small-angle X-ray scattering studies of LRP6PE1PE2PE3PE4, in isolation and in complex with Dkk1, plus negative-stain EM of full-length LRP6 ectodomain, have indicated curved, platform-like conformations but also potential flexibility between PE2 and PE3. RESULTS |
|
177 187 ectodomain structure_element Low-resolution negative-stain EM and small-angle X-ray scattering studies of LRP6PE1PE2PE3PE4, in isolation and in complex with Dkk1, plus negative-stain EM of full-length LRP6 ectodomain, have indicated curved, platform-like conformations but also potential flexibility between PE2 and PE3. RESULTS |
|
204 210 curved protein_state Low-resolution negative-stain EM and small-angle X-ray scattering studies of LRP6PE1PE2PE3PE4, in isolation and in complex with Dkk1, plus negative-stain EM of full-length LRP6 ectodomain, have indicated curved, platform-like conformations but also potential flexibility between PE2 and PE3. RESULTS |
|
212 225 platform-like protein_state Low-resolution negative-stain EM and small-angle X-ray scattering studies of LRP6PE1PE2PE3PE4, in isolation and in complex with Dkk1, plus negative-stain EM of full-length LRP6 ectodomain, have indicated curved, platform-like conformations but also potential flexibility between PE2 and PE3. RESULTS |
|
279 282 PE2 structure_element Low-resolution negative-stain EM and small-angle X-ray scattering studies of LRP6PE1PE2PE3PE4, in isolation and in complex with Dkk1, plus negative-stain EM of full-length LRP6 ectodomain, have indicated curved, platform-like conformations but also potential flexibility between PE2 and PE3. RESULTS |
|
287 290 PE3 structure_element Low-resolution negative-stain EM and small-angle X-ray scattering studies of LRP6PE1PE2PE3PE4, in isolation and in complex with Dkk1, plus negative-stain EM of full-length LRP6 ectodomain, have indicated curved, platform-like conformations but also potential flexibility between PE2 and PE3. RESULTS |
|
47 50 Krm protein_type It is therefore possible that the interplay of Krm and Dkk binding can promote changes in LRP6 ectodomain conformation with functional consequences |
|
55 58 Dkk protein_type It is therefore possible that the interplay of Krm and Dkk binding can promote changes in LRP6 ectodomain conformation with functional consequences |
|
90 94 LRP6 protein It is therefore possible that the interplay of Krm and Dkk binding can promote changes in LRP6 ectodomain conformation with functional consequences |
|
95 105 ectodomain structure_element It is therefore possible that the interplay of Krm and Dkk binding can promote changes in LRP6 ectodomain conformation with functional consequences |
|
20 54 structural and biophysical studies experimental_method Taken together, the structural and biophysical studies we report here extend our mechanistic understanding of Wnt signal regulation. RESULTS |
|
110 113 Wnt protein_type Taken together, the structural and biophysical studies we report here extend our mechanistic understanding of Wnt signal regulation. RESULTS |
|
16 26 ectodomain structure_element We describe the ectodomain structure of the dual Wnt regulator Krm1, providing an explanation for the detrimental effect on health and development of a homozygous KRM1 mutation. RESULTS |
|
27 36 structure evidence We describe the ectodomain structure of the dual Wnt regulator Krm1, providing an explanation for the detrimental effect on health and development of a homozygous KRM1 mutation. RESULTS |
|
49 52 Wnt protein_type We describe the ectodomain structure of the dual Wnt regulator Krm1, providing an explanation for the detrimental effect on health and development of a homozygous KRM1 mutation. RESULTS |
|
63 67 Krm1 protein_type We describe the ectodomain structure of the dual Wnt regulator Krm1, providing an explanation for the detrimental effect on health and development of a homozygous KRM1 mutation. RESULTS |
|
163 167 KRM1 protein We describe the ectodomain structure of the dual Wnt regulator Krm1, providing an explanation for the detrimental effect on health and development of a homozygous KRM1 mutation. RESULTS |
|
39 46 Krm-Dkk complex_assembly We also reveal the interaction mode of Krm-Dkk and the architecture of the ternary complex formed by Lrp5/6, Dkk, and Krm. RESULTS |
|
101 107 Lrp5/6 protein_type We also reveal the interaction mode of Krm-Dkk and the architecture of the ternary complex formed by Lrp5/6, Dkk, and Krm. RESULTS |
|
109 112 Dkk protein_type We also reveal the interaction mode of Krm-Dkk and the architecture of the ternary complex formed by Lrp5/6, Dkk, and Krm. RESULTS |
|
118 121 Krm protein_type We also reveal the interaction mode of Krm-Dkk and the architecture of the ternary complex formed by Lrp5/6, Dkk, and Krm. RESULTS |
|
25 42 crystal structure evidence Furthermore, the ternary crystal structure has guided inΒ silico and biophysical analyses to suggest a direct LRP6-KRM1 interaction site. RESULTS |
|
54 88 inΒ silico and biophysical analyses experimental_method Furthermore, the ternary crystal structure has guided inΒ silico and biophysical analyses to suggest a direct LRP6-KRM1 interaction site. RESULTS |
|
109 135 LRP6-KRM1 interaction site site Furthermore, the ternary crystal structure has guided inΒ silico and biophysical analyses to suggest a direct LRP6-KRM1 interaction site. RESULTS |
|
136 139 Krm protein_type Our findings provide a solid foundation for additional studies to probe how ternary complex formation triggers internalization, whereas Krm binding in the absence of Dkk stabilizes the Wnt co-receptor at the cell surface. RESULTS |
|
155 165 absence of protein_state Our findings provide a solid foundation for additional studies to probe how ternary complex formation triggers internalization, whereas Krm binding in the absence of Dkk stabilizes the Wnt co-receptor at the cell surface. RESULTS |
|
166 169 Dkk protein_type Our findings provide a solid foundation for additional studies to probe how ternary complex formation triggers internalization, whereas Krm binding in the absence of Dkk stabilizes the Wnt co-receptor at the cell surface. RESULTS |
|
185 188 Wnt protein_type Our findings provide a solid foundation for additional studies to probe how ternary complex formation triggers internalization, whereas Krm binding in the absence of Dkk stabilizes the Wnt co-receptor at the cell surface. RESULTS |
|
189 200 co-receptor protein_type Our findings provide a solid foundation for additional studies to probe how ternary complex formation triggers internalization, whereas Krm binding in the absence of Dkk stabilizes the Wnt co-receptor at the cell surface. RESULTS |
|
0 9 Structure evidence Structure of Unliganded KRM1ECD FIG |
|
13 23 Unliganded protein_state Structure of Unliganded KRM1ECD FIG |
|
24 28 KRM1 protein Structure of Unliganded KRM1ECD FIG |
|
28 31 ECD structure_element Structure of Unliganded KRM1ECD FIG |
|
8 12 KRM1 protein (A) The KRM1ECD fold (crystal form I) colored blue to red from the N to C terminus. FIG |
|
12 15 ECD structure_element (A) The KRM1ECD fold (crystal form I) colored blue to red from the N to C terminus. FIG |
|
22 36 crystal form I evidence (A) The KRM1ECD fold (crystal form I) colored blue to red from the N to C terminus. FIG |
|
0 9 Cysteines residue_name Cysteines as ball and sticks, glycosylation sites as sticks. FIG |
|
30 49 glycosylation sites site Cysteines as ball and sticks, glycosylation sites as sticks. FIG |
|
10 17 calcium chemical The bound calcium is shown as a gray sphere. FIG |
|
16 21 F207S mutant The site of theΒ F207S mutation associated with ectodermal dysplasia in humans is shown as mesh. FIG |
|
71 77 humans species The site of theΒ F207S mutation associated with ectodermal dysplasia in humans is shown as mesh. FIG |
|
4 17 Superposition experimental_method (B) Superposition of the three KRM1ECD subdomains (solid) with their next structurally characterized homologs (half transparent). FIG |
|
31 35 KRM1 protein (B) Superposition of the three KRM1ECD subdomains (solid) with their next structurally characterized homologs (half transparent). FIG |
|
35 38 ECD structure_element (B) Superposition of the three KRM1ECD subdomains (solid) with their next structurally characterized homologs (half transparent). FIG |
|
4 17 Superposition experimental_method (C) Superposition of KRM1ECD from the three crystal forms. FIG |
|
21 25 KRM1 protein (C) Superposition of KRM1ECD from the three crystal forms. FIG |
|
25 28 ECD structure_element (C) Superposition of KRM1ECD from the three crystal forms. FIG |
|
44 57 crystal forms evidence (C) Superposition of KRM1ECD from the three crystal forms. FIG |
|
0 16 Alignment scores evidence Alignment scores for each pairing are indicated on the dashed triangle. FIG |
|
8 17 structure evidence (A) The structure of the ternary LRP6PE3PE4-DKK1CRD2-KRM1ECD complex. FIG |
|
33 60 LRP6PE3PE4-DKK1CRD2-KRM1ECD complex_assembly (A) The structure of the ternary LRP6PE3PE4-DKK1CRD2-KRM1ECD complex. FIG |
|
0 4 DKK1 protein DKK1 (orange) is sandwiched between the PE3 module of LRP6 (blue) and the KR-WSC domain pair of KRM1 (green). FIG |
|
40 43 PE3 structure_element DKK1 (orange) is sandwiched between the PE3 module of LRP6 (blue) and the KR-WSC domain pair of KRM1 (green). FIG |
|
54 58 LRP6 protein DKK1 (orange) is sandwiched between the PE3 module of LRP6 (blue) and the KR-WSC domain pair of KRM1 (green). FIG |
|
74 80 KR-WSC structure_element DKK1 (orange) is sandwiched between the PE3 module of LRP6 (blue) and the KR-WSC domain pair of KRM1 (green). FIG |
|
96 100 KRM1 protein DKK1 (orange) is sandwiched between the PE3 module of LRP6 (blue) and the KR-WSC domain pair of KRM1 (green). FIG |
|
36 61 N-glycan attachment sites site Colored symbols indicate introduced N-glycan attachment sites (see D). FIG |
|
4 7 SPR experimental_method (B) SPR data comparing binding of full-length DKK1 and SUMO fusions of DKK1 truncations for binding to immobilized wild-type KRM1ECD. FIG |
|
34 45 full-length protein_state (B) SPR data comparing binding of full-length DKK1 and SUMO fusions of DKK1 truncations for binding to immobilized wild-type KRM1ECD. FIG |
|
46 50 DKK1 protein (B) SPR data comparing binding of full-length DKK1 and SUMO fusions of DKK1 truncations for binding to immobilized wild-type KRM1ECD. FIG |
|
55 67 SUMO fusions experimental_method (B) SPR data comparing binding of full-length DKK1 and SUMO fusions of DKK1 truncations for binding to immobilized wild-type KRM1ECD. FIG |
|
71 75 DKK1 protein (B) SPR data comparing binding of full-length DKK1 and SUMO fusions of DKK1 truncations for binding to immobilized wild-type KRM1ECD. FIG |
|
115 124 wild-type protein_state (B) SPR data comparing binding of full-length DKK1 and SUMO fusions of DKK1 truncations for binding to immobilized wild-type KRM1ECD. FIG |
|
125 129 KRM1 protein (B) SPR data comparing binding of full-length DKK1 and SUMO fusions of DKK1 truncations for binding to immobilized wild-type KRM1ECD. FIG |
|
129 132 ECD structure_element (B) SPR data comparing binding of full-length DKK1 and SUMO fusions of DKK1 truncations for binding to immobilized wild-type KRM1ECD. FIG |
|
25 51 DKK1CRD2-KRM1ECD interface site (C) Close-up view of the DKK1CRD2-KRM1ECD interface. FIG |
|
21 30 interface site Residues involved in interface formation are shown as sticks |
|
0 12 Salt bridges bond_interaction Salt bridges are in pink and hydrogen bonds in black. FIG |
|
29 43 hydrogen bonds bond_interaction Salt bridges are in pink and hydrogen bonds in black. FIG |
|
4 7 SPR experimental_method (D) SPR binding data comparing DKK1 analyte binding with wild-type KRM1ECD and three variants bearing engineered glycosylation sites on the KR and WSC domains (green and blue pointing to DKK1) and on the CUB domain (orange). FIG |
|
8 20 binding data evidence (D) SPR binding data comparing DKK1 analyte binding with wild-type KRM1ECD and three variants bearing engineered glycosylation sites on the KR and WSC domains (green and blue pointing to DKK1) and on the CUB domain (orange). FIG |
|
31 35 DKK1 protein (D) SPR binding data comparing DKK1 analyte binding with wild-type KRM1ECD and three variants bearing engineered glycosylation sites on the KR and WSC domains (green and blue pointing to DKK1) and on the CUB domain (orange). FIG |
|
57 66 wild-type protein_state (D) SPR binding data comparing DKK1 analyte binding with wild-type KRM1ECD and three variants bearing engineered glycosylation sites on the KR and WSC domains (green and blue pointing to DKK1) and on the CUB domain (orange). FIG |
|
67 71 KRM1 protein (D) SPR binding data comparing DKK1 analyte binding with wild-type KRM1ECD and three variants bearing engineered glycosylation sites on the KR and WSC domains (green and blue pointing to DKK1) and on the CUB domain (orange). FIG |
|
71 74 ECD structure_element (D) SPR binding data comparing DKK1 analyte binding with wild-type KRM1ECD and three variants bearing engineered glycosylation sites on the KR and WSC domains (green and blue pointing to DKK1) and on the CUB domain (orange). FIG |
|
102 112 engineered protein_state (D) SPR binding data comparing DKK1 analyte binding with wild-type KRM1ECD and three variants bearing engineered glycosylation sites on the KR and WSC domains (green and blue pointing to DKK1) and on the CUB domain (orange). FIG |
|
113 132 glycosylation sites site (D) SPR binding data comparing DKK1 analyte binding with wild-type KRM1ECD and three variants bearing engineered glycosylation sites on the KR and WSC domains (green and blue pointing to DKK1) and on the CUB domain (orange). FIG |
|
140 142 KR structure_element (D) SPR binding data comparing DKK1 analyte binding with wild-type KRM1ECD and three variants bearing engineered glycosylation sites on the KR and WSC domains (green and blue pointing to DKK1) and on the CUB domain (orange). FIG |
|
147 150 WSC structure_element (D) SPR binding data comparing DKK1 analyte binding with wild-type KRM1ECD and three variants bearing engineered glycosylation sites on the KR and WSC domains (green and blue pointing to DKK1) and on the CUB domain (orange). FIG |
|
187 191 DKK1 protein (D) SPR binding data comparing DKK1 analyte binding with wild-type KRM1ECD and three variants bearing engineered glycosylation sites on the KR and WSC domains (green and blue pointing to DKK1) and on the CUB domain (orange). FIG |
|
204 207 CUB structure_element (D) SPR binding data comparing DKK1 analyte binding with wild-type KRM1ECD and three variants bearing engineered glycosylation sites on the KR and WSC domains (green and blue pointing to DKK1) and on the CUB domain (orange). FIG |
|
0 9 LRP6-KRM1 complex_assembly LRP6-KRM1 Direct Interaction and Summary FIG |
|
35 47 complex with protein_state (A) In a construction of a ternary complex with all four Ξ² propellers of LRP6 intact, the CUB domain points via its Ca2+-binding region toward the top face of the second Ξ² propeller. FIG |
|
57 69 Ξ² propellers structure_element (A) In a construction of a ternary complex with all four Ξ² propellers of LRP6 intact, the CUB domain points via its Ca2+-binding region toward the top face of the second Ξ² propeller. FIG |
|
73 77 LRP6 protein (A) In a construction of a ternary complex with all four Ξ² propellers of LRP6 intact, the CUB domain points via its Ca2+-binding region toward the top face of the second Ξ² propeller. FIG |
|
78 84 intact protein_state (A) In a construction of a ternary complex with all four Ξ² propellers of LRP6 intact, the CUB domain points via its Ca2+-binding region toward the top face of the second Ξ² propeller. FIG |
|
90 93 CUB structure_element (A) In a construction of a ternary complex with all four Ξ² propellers of LRP6 intact, the CUB domain points via its Ca2+-binding region toward the top face of the second Ξ² propeller. FIG |
|
116 135 Ca2+-binding region site (A) In a construction of a ternary complex with all four Ξ² propellers of LRP6 intact, the CUB domain points via its Ca2+-binding region toward the top face of the second Ξ² propeller. FIG |
|
163 181 second Ξ² propeller structure_element (A) In a construction of a ternary complex with all four Ξ² propellers of LRP6 intact, the CUB domain points via its Ca2+-binding region toward the top face of the second Ξ² propeller. FIG |
|
35 51 interaction site site (B) Close-up view of the potential interaction site. FIG |
|
13 17 LRP6 protein In addition, LRP6PE2 has been superimposed with DKK1 (yellow) and SOST (pink) peptide complexes of LRP6PE1. FIG |
|
17 20 PE2 structure_element In addition, LRP6PE2 has been superimposed with DKK1 (yellow) and SOST (pink) peptide complexes of LRP6PE1. FIG |
|
30 42 superimposed experimental_method In addition, LRP6PE2 has been superimposed with DKK1 (yellow) and SOST (pink) peptide complexes of LRP6PE1. FIG |
|
48 52 DKK1 protein In addition, LRP6PE2 has been superimposed with DKK1 (yellow) and SOST (pink) peptide complexes of LRP6PE1. FIG |
|
66 70 SOST protein In addition, LRP6PE2 has been superimposed with DKK1 (yellow) and SOST (pink) peptide complexes of LRP6PE1. FIG |
|
99 103 LRP6 protein In addition, LRP6PE2 has been superimposed with DKK1 (yellow) and SOST (pink) peptide complexes of LRP6PE1. FIG |
|
103 106 PE1 structure_element In addition, LRP6PE2 has been superimposed with DKK1 (yellow) and SOST (pink) peptide complexes of LRP6PE1. FIG |
|
4 20 SPR measurements experimental_method (C) SPR measurements comparing LRP6PE1PE2 binding with wild-type KRM1ECD and the GlycoCUB mutant bearing an N-glycan at N309. FIG |
|
31 35 LRP6 protein (C) SPR measurements comparing LRP6PE1PE2 binding with wild-type KRM1ECD and the GlycoCUB mutant bearing an N-glycan at N309. FIG |
|
35 41 PE1PE2 structure_element (C) SPR measurements comparing LRP6PE1PE2 binding with wild-type KRM1ECD and the GlycoCUB mutant bearing an N-glycan at N309. FIG |
|
55 64 wild-type protein_state (C) SPR measurements comparing LRP6PE1PE2 binding with wild-type KRM1ECD and the GlycoCUB mutant bearing an N-glycan at N309. FIG |
|
65 69 KRM1 protein (C) SPR measurements comparing LRP6PE1PE2 binding with wild-type KRM1ECD and the GlycoCUB mutant bearing an N-glycan at N309. FIG |
|
69 72 ECD structure_element (C) SPR measurements comparing LRP6PE1PE2 binding with wild-type KRM1ECD and the GlycoCUB mutant bearing an N-glycan at N309. FIG |
|
81 96 GlycoCUB mutant protein_state (C) SPR measurements comparing LRP6PE1PE2 binding with wild-type KRM1ECD and the GlycoCUB mutant bearing an N-glycan at N309. FIG |
|
108 116 N-glycan ptm (C) SPR measurements comparing LRP6PE1PE2 binding with wild-type KRM1ECD and the GlycoCUB mutant bearing an N-glycan at N309. FIG |
|
120 124 N309 residue_name_number (C) SPR measurements comparing LRP6PE1PE2 binding with wild-type KRM1ECD and the GlycoCUB mutant bearing an N-glycan at N309. FIG |
|
95 98 Wnt protein_type (D) Schematic representation of structural and biophysical findings and their implications for Wnt-dependent (left, middle) and independent (right) signaling. FIG |
|
48 52 LRP6 protein Conformational differences in the depictions of LRP6 are included purely for ease of representation. FIG |
|
0 37 Diffraction and Refinement Statistics evidence Diffraction and Refinement Statistics TABLE |
|
1 5 KRM1 protein " KRM1ECD KRM1ECD KRM1ECD KRM1ECD LRP6PE3PE4-DKKCRD2-KRM1ECD Crystal form I I II III I X-ray source Diamond i04 Diamond i03 Diamond i03 Diamond i04 Diamond i04 Wavelength (Γ
) 0.9793 0.9700 0.9700 0.9795 0.9795 Space group P3121 P3121 P43 P41212 C2221 Unit cell a/Ξ± (Γ
/Β°) 50.9/90 50.5/90 65.8/90 67.8/90 86.9/90 b/Ξ² (Γ
/Β°) 50.9/90 50.5/90 65.8/90 67.8/90 100.1/90 c/Ξ³ (Γ
/Β°) 188.4/120 187.4/120 75.0/90 198.2/90 270.7/90 Wilson B factor (Γ
2) 31 41 76 77 NA Resolution range (Γ
) 47.10β1.90 (1.95β1.90) 62.47β2.10 (2.16β2.10) 75.00β2.80 (2.99β2.80) 67.80β3.20 (3.42β3.20) 67.68β3.50 (7.16β6.40, 3.92β3.50) Unique reflections 23,300 (1,524) 17,089 (1,428) 7,964 (1,448) 8,171 (1,343) 8,070 (723, 645) Average multiplicity 9.1 (9.2) 5.2 (5.3) 3.7 (3.7) 22.7 (12.6) 3.8 (3.5, 4.4) Completeness (%) 99.8 (98.5) 100 (100) 99.8 (100) 98.8 (93.4) 51.6 (98.5, 14.1) <I/ΟI> 11.4 (1.7) 12.0 (1.7) 14.9 (1.5) 13.1 (1.9) 4.6 (4.1, 2.2) Rmerge (%) 14.8 (158.3) 9.3 (98.0) 6.2 (98.9) 29.8 (142.2) 44.9 (40.5, 114.2) Rpim (%) 15.7 (55.3) 10.3 (109.0) 3.7 (53.8) 6.3 (40.0) 24.7 (23.9, 59.9) Refinement Rwork (%) 17.9 18.4 21.6 20.2 32.1 Rfree (%) 22.7 23.2 30.7 27.1 35.5 No. of Non-Hydrogen Atoms Protein 2,260 2,301 2,102 2,305 7,730 N-glycans 42 42 28 28 0 Water 79 54 0 2 0 Ligands 6 6 2 5 0 Average B factor (Γ
2) Protein 63 65 108 84 β N-glycans 35 46 102 18 β Water 68 85 β 75 β Ligands 36 47 91 75 66 RMSD from Ideality Bond lengths (Γ
) 0.020 0.016 0.019 0.016 0.004 Bond angles (Β°) 2.050 1.748 1.952 1.796 0.770 Ramachandran Plot Favored (%) 96.8 95.5 96.9 94.9 92.3 Allowed (%) 99.7 100.0 100.0 99.7 99.8 Number of outliers 1 0 0 1 2 PDB code 5FWS 5FWT 5FWU 5FWV 5FWW " TABLE |
|
5 8 ECD structure_element " KRM1ECD KRM1ECD KRM1ECD KRM1ECD LRP6PE3PE4-DKKCRD2-KRM1ECD Crystal form I I II III I X-ray source Diamond i04 Diamond i03 Diamond i03 Diamond i04 Diamond i04 Wavelength (Γ
) 0.9793 0.9700 0.9700 0.9795 0.9795 Space group P3121 P3121 P43 P41212 C2221 Unit cell a/Ξ± (Γ
/Β°) 50.9/90 50.5/90 65.8/90 67.8/90 86.9/90 b/Ξ² (Γ
/Β°) 50.9/90 50.5/90 65.8/90 67.8/90 100.1/90 c/Ξ³ (Γ
/Β°) 188.4/120 187.4/120 75.0/90 198.2/90 270.7/90 Wilson B factor (Γ
2) 31 41 76 77 NA Resolution range (Γ
) 47.10β1.90 (1.95β1.90) 62.47β2.10 (2.16β2.10) 75.00β2.80 (2.99β2.80) 67.80β3.20 (3.42β3.20) 67.68β3.50 (7.16β6.40, 3.92β3.50) Unique reflections 23,300 (1,524) 17,089 (1,428) 7,964 (1,448) 8,171 (1,343) 8,070 (723, 645) Average multiplicity 9.1 (9.2) 5.2 (5.3) 3.7 (3.7) 22.7 (12.6) 3.8 (3.5, 4.4) Completeness (%) 99.8 (98.5) 100 (100) 99.8 (100) 98.8 (93.4) 51.6 (98.5, 14.1) <I/ΟI> 11.4 (1.7) 12.0 (1.7) 14.9 (1.5) 13.1 (1.9) 4.6 (4.1, 2.2) Rmerge (%) 14.8 (158.3) 9.3 (98.0) 6.2 (98.9) 29.8 (142.2) 44.9 (40.5, 114.2) Rpim (%) 15.7 (55.3) 10.3 (109.0) 3.7 (53.8) 6.3 (40.0) 24.7 (23.9, 59.9) Refinement Rwork (%) 17.9 18.4 21.6 20.2 32.1 Rfree (%) 22.7 23.2 30.7 27.1 35.5 No. of Non-Hydrogen Atoms Protein 2,260 2,301 2,102 2,305 7,730 N-glycans 42 42 28 28 0 Water 79 54 0 2 0 Ligands 6 6 2 5 0 Average B factor (Γ
2) Protein 63 65 108 84 β N-glycans 35 46 102 18 β Water 68 85 β 75 β Ligands 36 47 91 75 66 RMSD from Ideality Bond lengths (Γ
) 0.020 0.016 0.019 0.016 0.004 Bond angles (Β°) 2.050 1.748 1.952 1.796 0.770 Ramachandran Plot Favored (%) 96.8 95.5 96.9 94.9 92.3 Allowed (%) 99.7 100.0 100.0 99.7 99.8 Number of outliers 1 0 0 1 2 PDB code 5FWS 5FWT 5FWU 5FWV 5FWW " TABLE |
|
9 13 KRM1 protein " KRM1ECD KRM1ECD KRM1ECD KRM1ECD LRP6PE3PE4-DKKCRD2-KRM1ECD Crystal form I I II III I X-ray source Diamond i04 Diamond i03 Diamond i03 Diamond i04 Diamond i04 Wavelength (Γ
) 0.9793 0.9700 0.9700 0.9795 0.9795 Space group P3121 P3121 P43 P41212 C2221 Unit cell a/Ξ± (Γ
/Β°) 50.9/90 50.5/90 65.8/90 67.8/90 86.9/90 b/Ξ² (Γ
/Β°) 50.9/90 50.5/90 65.8/90 67.8/90 100.1/90 c/Ξ³ (Γ
/Β°) 188.4/120 187.4/120 75.0/90 198.2/90 270.7/90 Wilson B factor (Γ
2) 31 41 76 77 NA Resolution range (Γ
) 47.10β1.90 (1.95β1.90) 62.47β2.10 (2.16β2.10) 75.00β2.80 (2.99β2.80) 67.80β3.20 (3.42β3.20) 67.68β3.50 (7.16β6.40, 3.92β3.50) Unique reflections 23,300 (1,524) 17,089 (1,428) 7,964 (1,448) 8,171 (1,343) 8,070 (723, 645) Average multiplicity 9.1 (9.2) 5.2 (5.3) 3.7 (3.7) 22.7 (12.6) 3.8 (3.5, 4.4) Completeness (%) 99.8 (98.5) 100 (100) 99.8 (100) 98.8 (93.4) 51.6 (98.5, 14.1) <I/ΟI> 11.4 (1.7) 12.0 (1.7) 14.9 (1.5) 13.1 (1.9) 4.6 (4.1, 2.2) Rmerge (%) 14.8 (158.3) 9.3 (98.0) 6.2 (98.9) 29.8 (142.2) 44.9 (40.5, 114.2) Rpim (%) 15.7 (55.3) 10.3 (109.0) 3.7 (53.8) 6.3 (40.0) 24.7 (23.9, 59.9) Refinement Rwork (%) 17.9 18.4 21.6 20.2 32.1 Rfree (%) 22.7 23.2 30.7 27.1 35.5 No. of Non-Hydrogen Atoms Protein 2,260 2,301 2,102 2,305 7,730 N-glycans 42 42 28 28 0 Water 79 54 0 2 0 Ligands 6 6 2 5 0 Average B factor (Γ
2) Protein 63 65 108 84 β N-glycans 35 46 102 18 β Water 68 85 β 75 β Ligands 36 47 91 75 66 RMSD from Ideality Bond lengths (Γ
) 0.020 0.016 0.019 0.016 0.004 Bond angles (Β°) 2.050 1.748 1.952 1.796 0.770 Ramachandran Plot Favored (%) 96.8 95.5 96.9 94.9 92.3 Allowed (%) 99.7 100.0 100.0 99.7 99.8 Number of outliers 1 0 0 1 2 PDB code 5FWS 5FWT 5FWU 5FWV 5FWW " TABLE |
|
13 16 ECD structure_element " KRM1ECD KRM1ECD KRM1ECD KRM1ECD LRP6PE3PE4-DKKCRD2-KRM1ECD Crystal form I I II III I X-ray source Diamond i04 Diamond i03 Diamond i03 Diamond i04 Diamond i04 Wavelength (Γ
) 0.9793 0.9700 0.9700 0.9795 0.9795 Space group P3121 P3121 P43 P41212 C2221 Unit cell a/Ξ± (Γ
/Β°) 50.9/90 50.5/90 65.8/90 67.8/90 86.9/90 b/Ξ² (Γ
/Β°) 50.9/90 50.5/90 65.8/90 67.8/90 100.1/90 c/Ξ³ (Γ
/Β°) 188.4/120 187.4/120 75.0/90 198.2/90 270.7/90 Wilson B factor (Γ
2) 31 41 76 77 NA Resolution range (Γ
) 47.10β1.90 (1.95β1.90) 62.47β2.10 (2.16β2.10) 75.00β2.80 (2.99β2.80) 67.80β3.20 (3.42β3.20) 67.68β3.50 (7.16β6.40, 3.92β3.50) Unique reflections 23,300 (1,524) 17,089 (1,428) 7,964 (1,448) 8,171 (1,343) 8,070 (723, 645) Average multiplicity 9.1 (9.2) 5.2 (5.3) 3.7 (3.7) 22.7 (12.6) 3.8 (3.5, 4.4) Completeness (%) 99.8 (98.5) 100 (100) 99.8 (100) 98.8 (93.4) 51.6 (98.5, 14.1) <I/ΟI> 11.4 (1.7) 12.0 (1.7) 14.9 (1.5) 13.1 (1.9) 4.6 (4.1, 2.2) Rmerge (%) 14.8 (158.3) 9.3 (98.0) 6.2 (98.9) 29.8 (142.2) 44.9 (40.5, 114.2) Rpim (%) 15.7 (55.3) 10.3 (109.0) 3.7 (53.8) 6.3 (40.0) 24.7 (23.9, 59.9) Refinement Rwork (%) 17.9 18.4 21.6 20.2 32.1 Rfree (%) 22.7 23.2 30.7 27.1 35.5 No. of Non-Hydrogen Atoms Protein 2,260 2,301 2,102 2,305 7,730 N-glycans 42 42 28 28 0 Water 79 54 0 2 0 Ligands 6 6 2 5 0 Average B factor (Γ
2) Protein 63 65 108 84 β N-glycans 35 46 102 18 β Water 68 85 β 75 β Ligands 36 47 91 75 66 RMSD from Ideality Bond lengths (Γ
) 0.020 0.016 0.019 0.016 0.004 Bond angles (Β°) 2.050 1.748 1.952 1.796 0.770 Ramachandran Plot Favored (%) 96.8 95.5 96.9 94.9 92.3 Allowed (%) 99.7 100.0 100.0 99.7 99.8 Number of outliers 1 0 0 1 2 PDB code 5FWS 5FWT 5FWU 5FWV 5FWW " TABLE |
|
17 21 KRM1 protein " KRM1ECD KRM1ECD KRM1ECD KRM1ECD LRP6PE3PE4-DKKCRD2-KRM1ECD Crystal form I I II III I X-ray source Diamond i04 Diamond i03 Diamond i03 Diamond i04 Diamond i04 Wavelength (Γ
) 0.9793 0.9700 0.9700 0.9795 0.9795 Space group P3121 P3121 P43 P41212 C2221 Unit cell a/Ξ± (Γ
/Β°) 50.9/90 50.5/90 65.8/90 67.8/90 86.9/90 b/Ξ² (Γ
/Β°) 50.9/90 50.5/90 65.8/90 67.8/90 100.1/90 c/Ξ³ (Γ
/Β°) 188.4/120 187.4/120 75.0/90 198.2/90 270.7/90 Wilson B factor (Γ
2) 31 41 76 77 NA Resolution range (Γ
) 47.10β1.90 (1.95β1.90) 62.47β2.10 (2.16β2.10) 75.00β2.80 (2.99β2.80) 67.80β3.20 (3.42β3.20) 67.68β3.50 (7.16β6.40, 3.92β3.50) Unique reflections 23,300 (1,524) 17,089 (1,428) 7,964 (1,448) 8,171 (1,343) 8,070 (723, 645) Average multiplicity 9.1 (9.2) 5.2 (5.3) 3.7 (3.7) 22.7 (12.6) 3.8 (3.5, 4.4) Completeness (%) 99.8 (98.5) 100 (100) 99.8 (100) 98.8 (93.4) 51.6 (98.5, 14.1) <I/ΟI> 11.4 (1.7) 12.0 (1.7) 14.9 (1.5) 13.1 (1.9) 4.6 (4.1, 2.2) Rmerge (%) 14.8 (158.3) 9.3 (98.0) 6.2 (98.9) 29.8 (142.2) 44.9 (40.5, 114.2) Rpim (%) 15.7 (55.3) 10.3 (109.0) 3.7 (53.8) 6.3 (40.0) 24.7 (23.9, 59.9) Refinement Rwork (%) 17.9 18.4 21.6 20.2 32.1 Rfree (%) 22.7 23.2 30.7 27.1 35.5 No. of Non-Hydrogen Atoms Protein 2,260 2,301 2,102 2,305 7,730 N-glycans 42 42 28 28 0 Water 79 54 0 2 0 Ligands 6 6 2 5 0 Average B factor (Γ
2) Protein 63 65 108 84 β N-glycans 35 46 102 18 β Water 68 85 β 75 β Ligands 36 47 91 75 66 RMSD from Ideality Bond lengths (Γ
) 0.020 0.016 0.019 0.016 0.004 Bond angles (Β°) 2.050 1.748 1.952 1.796 0.770 Ramachandran Plot Favored (%) 96.8 95.5 96.9 94.9 92.3 Allowed (%) 99.7 100.0 100.0 99.7 99.8 Number of outliers 1 0 0 1 2 PDB code 5FWS 5FWT 5FWU 5FWV 5FWW " TABLE |
|
21 24 ECD structure_element " KRM1ECD KRM1ECD KRM1ECD KRM1ECD LRP6PE3PE4-DKKCRD2-KRM1ECD Crystal form I I II III I X-ray source Diamond i04 Diamond i03 Diamond i03 Diamond i04 Diamond i04 Wavelength (Γ
) 0.9793 0.9700 0.9700 0.9795 0.9795 Space group P3121 P3121 P43 P41212 C2221 Unit cell a/Ξ± (Γ
/Β°) 50.9/90 50.5/90 65.8/90 67.8/90 86.9/90 b/Ξ² (Γ
/Β°) 50.9/90 50.5/90 65.8/90 67.8/90 100.1/90 c/Ξ³ (Γ
/Β°) 188.4/120 187.4/120 75.0/90 198.2/90 270.7/90 Wilson B factor (Γ
2) 31 41 76 77 NA Resolution range (Γ
) 47.10β1.90 (1.95β1.90) 62.47β2.10 (2.16β2.10) 75.00β2.80 (2.99β2.80) 67.80β3.20 (3.42β3.20) 67.68β3.50 (7.16β6.40, 3.92β3.50) Unique reflections 23,300 (1,524) 17,089 (1,428) 7,964 (1,448) 8,171 (1,343) 8,070 (723, 645) Average multiplicity 9.1 (9.2) 5.2 (5.3) 3.7 (3.7) 22.7 (12.6) 3.8 (3.5, 4.4) Completeness (%) 99.8 (98.5) 100 (100) 99.8 (100) 98.8 (93.4) 51.6 (98.5, 14.1) <I/ΟI> 11.4 (1.7) 12.0 (1.7) 14.9 (1.5) 13.1 (1.9) 4.6 (4.1, 2.2) Rmerge (%) 14.8 (158.3) 9.3 (98.0) 6.2 (98.9) 29.8 (142.2) 44.9 (40.5, 114.2) Rpim (%) 15.7 (55.3) 10.3 (109.0) 3.7 (53.8) 6.3 (40.0) 24.7 (23.9, 59.9) Refinement Rwork (%) 17.9 18.4 21.6 20.2 32.1 Rfree (%) 22.7 23.2 30.7 27.1 35.5 No. of Non-Hydrogen Atoms Protein 2,260 2,301 2,102 2,305 7,730 N-glycans 42 42 28 28 0 Water 79 54 0 2 0 Ligands 6 6 2 5 0 Average B factor (Γ
2) Protein 63 65 108 84 β N-glycans 35 46 102 18 β Water 68 85 β 75 β Ligands 36 47 91 75 66 RMSD from Ideality Bond lengths (Γ
) 0.020 0.016 0.019 0.016 0.004 Bond angles (Β°) 2.050 1.748 1.952 1.796 0.770 Ramachandran Plot Favored (%) 96.8 95.5 96.9 94.9 92.3 Allowed (%) 99.7 100.0 100.0 99.7 99.8 Number of outliers 1 0 0 1 2 PDB code 5FWS 5FWT 5FWU 5FWV 5FWW " TABLE |
|
25 29 KRM1 protein " KRM1ECD KRM1ECD KRM1ECD KRM1ECD LRP6PE3PE4-DKKCRD2-KRM1ECD Crystal form I I II III I X-ray source Diamond i04 Diamond i03 Diamond i03 Diamond i04 Diamond i04 Wavelength (Γ
) 0.9793 0.9700 0.9700 0.9795 0.9795 Space group P3121 P3121 P43 P41212 C2221 Unit cell a/Ξ± (Γ
/Β°) 50.9/90 50.5/90 65.8/90 67.8/90 86.9/90 b/Ξ² (Γ
/Β°) 50.9/90 50.5/90 65.8/90 67.8/90 100.1/90 c/Ξ³ (Γ
/Β°) 188.4/120 187.4/120 75.0/90 198.2/90 270.7/90 Wilson B factor (Γ
2) 31 41 76 77 NA Resolution range (Γ
) 47.10β1.90 (1.95β1.90) 62.47β2.10 (2.16β2.10) 75.00β2.80 (2.99β2.80) 67.80β3.20 (3.42β3.20) 67.68β3.50 (7.16β6.40, 3.92β3.50) Unique reflections 23,300 (1,524) 17,089 (1,428) 7,964 (1,448) 8,171 (1,343) 8,070 (723, 645) Average multiplicity 9.1 (9.2) 5.2 (5.3) 3.7 (3.7) 22.7 (12.6) 3.8 (3.5, 4.4) Completeness (%) 99.8 (98.5) 100 (100) 99.8 (100) 98.8 (93.4) 51.6 (98.5, 14.1) <I/ΟI> 11.4 (1.7) 12.0 (1.7) 14.9 (1.5) 13.1 (1.9) 4.6 (4.1, 2.2) Rmerge (%) 14.8 (158.3) 9.3 (98.0) 6.2 (98.9) 29.8 (142.2) 44.9 (40.5, 114.2) Rpim (%) 15.7 (55.3) 10.3 (109.0) 3.7 (53.8) 6.3 (40.0) 24.7 (23.9, 59.9) Refinement Rwork (%) 17.9 18.4 21.6 20.2 32.1 Rfree (%) 22.7 23.2 30.7 27.1 35.5 No. of Non-Hydrogen Atoms Protein 2,260 2,301 2,102 2,305 7,730 N-glycans 42 42 28 28 0 Water 79 54 0 2 0 Ligands 6 6 2 5 0 Average B factor (Γ
2) Protein 63 65 108 84 β N-glycans 35 46 102 18 β Water 68 85 β 75 β Ligands 36 47 91 75 66 RMSD from Ideality Bond lengths (Γ
) 0.020 0.016 0.019 0.016 0.004 Bond angles (Β°) 2.050 1.748 1.952 1.796 0.770 Ramachandran Plot Favored (%) 96.8 95.5 96.9 94.9 92.3 Allowed (%) 99.7 100.0 100.0 99.7 99.8 Number of outliers 1 0 0 1 2 PDB code 5FWS 5FWT 5FWU 5FWV 5FWW " TABLE |
|
29 32 ECD structure_element " KRM1ECD KRM1ECD KRM1ECD KRM1ECD LRP6PE3PE4-DKKCRD2-KRM1ECD Crystal form I I II III I X-ray source Diamond i04 Diamond i03 Diamond i03 Diamond i04 Diamond i04 Wavelength (Γ
) 0.9793 0.9700 0.9700 0.9795 0.9795 Space group P3121 P3121 P43 P41212 C2221 Unit cell a/Ξ± (Γ
/Β°) 50.9/90 50.5/90 65.8/90 67.8/90 86.9/90 b/Ξ² (Γ
/Β°) 50.9/90 50.5/90 65.8/90 67.8/90 100.1/90 c/Ξ³ (Γ
/Β°) 188.4/120 187.4/120 75.0/90 198.2/90 270.7/90 Wilson B factor (Γ
2) 31 41 76 77 NA Resolution range (Γ
) 47.10β1.90 (1.95β1.90) 62.47β2.10 (2.16β2.10) 75.00β2.80 (2.99β2.80) 67.80β3.20 (3.42β3.20) 67.68β3.50 (7.16β6.40, 3.92β3.50) Unique reflections 23,300 (1,524) 17,089 (1,428) 7,964 (1,448) 8,171 (1,343) 8,070 (723, 645) Average multiplicity 9.1 (9.2) 5.2 (5.3) 3.7 (3.7) 22.7 (12.6) 3.8 (3.5, 4.4) Completeness (%) 99.8 (98.5) 100 (100) 99.8 (100) 98.8 (93.4) 51.6 (98.5, 14.1) <I/ΟI> 11.4 (1.7) 12.0 (1.7) 14.9 (1.5) 13.1 (1.9) 4.6 (4.1, 2.2) Rmerge (%) 14.8 (158.3) 9.3 (98.0) 6.2 (98.9) 29.8 (142.2) 44.9 (40.5, 114.2) Rpim (%) 15.7 (55.3) 10.3 (109.0) 3.7 (53.8) 6.3 (40.0) 24.7 (23.9, 59.9) Refinement Rwork (%) 17.9 18.4 21.6 20.2 32.1 Rfree (%) 22.7 23.2 30.7 27.1 35.5 No. of Non-Hydrogen Atoms Protein 2,260 2,301 2,102 2,305 7,730 N-glycans 42 42 28 28 0 Water 79 54 0 2 0 Ligands 6 6 2 5 0 Average B factor (Γ
2) Protein 63 65 108 84 β N-glycans 35 46 102 18 β Water 68 85 β 75 β Ligands 36 47 91 75 66 RMSD from Ideality Bond lengths (Γ
) 0.020 0.016 0.019 0.016 0.004 Bond angles (Β°) 2.050 1.748 1.952 1.796 0.770 Ramachandran Plot Favored (%) 96.8 95.5 96.9 94.9 92.3 Allowed (%) 99.7 100.0 100.0 99.7 99.8 Number of outliers 1 0 0 1 2 PDB code 5FWS 5FWT 5FWU 5FWV 5FWW " TABLE |
|
33 59 LRP6PE3PE4-DKKCRD2-KRM1ECD complex_assembly " KRM1ECD KRM1ECD KRM1ECD KRM1ECD LRP6PE3PE4-DKKCRD2-KRM1ECD Crystal form I I II III I X-ray source Diamond i04 Diamond i03 Diamond i03 Diamond i04 Diamond i04 Wavelength (Γ
) 0.9793 0.9700 0.9700 0.9795 0.9795 Space group P3121 P3121 P43 P41212 C2221 Unit cell a/Ξ± (Γ
/Β°) 50.9/90 50.5/90 65.8/90 67.8/90 86.9/90 b/Ξ² (Γ
/Β°) 50.9/90 50.5/90 65.8/90 67.8/90 100.1/90 c/Ξ³ (Γ
/Β°) 188.4/120 187.4/120 75.0/90 198.2/90 270.7/90 Wilson B factor (Γ
2) 31 41 76 77 NA Resolution range (Γ
) 47.10β1.90 (1.95β1.90) 62.47β2.10 (2.16β2.10) 75.00β2.80 (2.99β2.80) 67.80β3.20 (3.42β3.20) 67.68β3.50 (7.16β6.40, 3.92β3.50) Unique reflections 23,300 (1,524) 17,089 (1,428) 7,964 (1,448) 8,171 (1,343) 8,070 (723, 645) Average multiplicity 9.1 (9.2) 5.2 (5.3) 3.7 (3.7) 22.7 (12.6) 3.8 (3.5, 4.4) Completeness (%) 99.8 (98.5) 100 (100) 99.8 (100) 98.8 (93.4) 51.6 (98.5, 14.1) <I/ΟI> 11.4 (1.7) 12.0 (1.7) 14.9 (1.5) 13.1 (1.9) 4.6 (4.1, 2.2) Rmerge (%) 14.8 (158.3) 9.3 (98.0) 6.2 (98.9) 29.8 (142.2) 44.9 (40.5, 114.2) Rpim (%) 15.7 (55.3) 10.3 (109.0) 3.7 (53.8) 6.3 (40.0) 24.7 (23.9, 59.9) Refinement Rwork (%) 17.9 18.4 21.6 20.2 32.1 Rfree (%) 22.7 23.2 30.7 27.1 35.5 No. of Non-Hydrogen Atoms Protein 2,260 2,301 2,102 2,305 7,730 N-glycans 42 42 28 28 0 Water 79 54 0 2 0 Ligands 6 6 2 5 0 Average B factor (Γ
2) Protein 63 65 108 84 β N-glycans 35 46 102 18 β Water 68 85 β 75 β Ligands 36 47 91 75 66 RMSD from Ideality Bond lengths (Γ
) 0.020 0.016 0.019 0.016 0.004 Bond angles (Β°) 2.050 1.748 1.952 1.796 0.770 Ramachandran Plot Favored (%) 96.8 95.5 96.9 94.9 92.3 Allowed (%) 99.7 100.0 100.0 99.7 99.8 Number of outliers 1 0 0 1 2 PDB code 5FWS 5FWT 5FWU 5FWV 5FWW " TABLE |
|
1295 1300 Water chemical " KRM1ECD KRM1ECD KRM1ECD KRM1ECD LRP6PE3PE4-DKKCRD2-KRM1ECD Crystal form I I II III I X-ray source Diamond i04 Diamond i03 Diamond i03 Diamond i04 Diamond i04 Wavelength (Γ
) 0.9793 0.9700 0.9700 0.9795 0.9795 Space group P3121 P3121 P43 P41212 C2221 Unit cell a/Ξ± (Γ
/Β°) 50.9/90 50.5/90 65.8/90 67.8/90 86.9/90 b/Ξ² (Γ
/Β°) 50.9/90 50.5/90 65.8/90 67.8/90 100.1/90 c/Ξ³ (Γ
/Β°) 188.4/120 187.4/120 75.0/90 198.2/90 270.7/90 Wilson B factor (Γ
2) 31 41 76 77 NA Resolution range (Γ
) 47.10β1.90 (1.95β1.90) 62.47β2.10 (2.16β2.10) 75.00β2.80 (2.99β2.80) 67.80β3.20 (3.42β3.20) 67.68β3.50 (7.16β6.40, 3.92β3.50) Unique reflections 23,300 (1,524) 17,089 (1,428) 7,964 (1,448) 8,171 (1,343) 8,070 (723, 645) Average multiplicity 9.1 (9.2) 5.2 (5.3) 3.7 (3.7) 22.7 (12.6) 3.8 (3.5, 4.4) Completeness (%) 99.8 (98.5) 100 (100) 99.8 (100) 98.8 (93.4) 51.6 (98.5, 14.1) <I/ΟI> 11.4 (1.7) 12.0 (1.7) 14.9 (1.5) 13.1 (1.9) 4.6 (4.1, 2.2) Rmerge (%) 14.8 (158.3) 9.3 (98.0) 6.2 (98.9) 29.8 (142.2) 44.9 (40.5, 114.2) Rpim (%) 15.7 (55.3) 10.3 (109.0) 3.7 (53.8) 6.3 (40.0) 24.7 (23.9, 59.9) Refinement Rwork (%) 17.9 18.4 21.6 20.2 32.1 Rfree (%) 22.7 23.2 30.7 27.1 35.5 No. of Non-Hydrogen Atoms Protein 2,260 2,301 2,102 2,305 7,730 N-glycans 42 42 28 28 0 Water 79 54 0 2 0 Ligands 6 6 2 5 0 Average B factor (Γ
2) Protein 63 65 108 84 β N-glycans 35 46 102 18 β Water 68 85 β 75 β Ligands 36 47 91 75 66 RMSD from Ideality Bond lengths (Γ
) 0.020 0.016 0.019 0.016 0.004 Bond angles (Β°) 2.050 1.748 1.952 1.796 0.770 Ramachandran Plot Favored (%) 96.8 95.5 96.9 94.9 92.3 Allowed (%) 99.7 100.0 100.0 99.7 99.8 Number of outliers 1 0 0 1 2 PDB code 5FWS 5FWT 5FWU 5FWV 5FWW " TABLE |
|
1417 1422 Water chemical " KRM1ECD KRM1ECD KRM1ECD KRM1ECD LRP6PE3PE4-DKKCRD2-KRM1ECD Crystal form I I II III I X-ray source Diamond i04 Diamond i03 Diamond i03 Diamond i04 Diamond i04 Wavelength (Γ
) 0.9793 0.9700 0.9700 0.9795 0.9795 Space group P3121 P3121 P43 P41212 C2221 Unit cell a/Ξ± (Γ
/Β°) 50.9/90 50.5/90 65.8/90 67.8/90 86.9/90 b/Ξ² (Γ
/Β°) 50.9/90 50.5/90 65.8/90 67.8/90 100.1/90 c/Ξ³ (Γ
/Β°) 188.4/120 187.4/120 75.0/90 198.2/90 270.7/90 Wilson B factor (Γ
2) 31 41 76 77 NA Resolution range (Γ
) 47.10β1.90 (1.95β1.90) 62.47β2.10 (2.16β2.10) 75.00β2.80 (2.99β2.80) 67.80β3.20 (3.42β3.20) 67.68β3.50 (7.16β6.40, 3.92β3.50) Unique reflections 23,300 (1,524) 17,089 (1,428) 7,964 (1,448) 8,171 (1,343) 8,070 (723, 645) Average multiplicity 9.1 (9.2) 5.2 (5.3) 3.7 (3.7) 22.7 (12.6) 3.8 (3.5, 4.4) Completeness (%) 99.8 (98.5) 100 (100) 99.8 (100) 98.8 (93.4) 51.6 (98.5, 14.1) <I/ΟI> 11.4 (1.7) 12.0 (1.7) 14.9 (1.5) 13.1 (1.9) 4.6 (4.1, 2.2) Rmerge (%) 14.8 (158.3) 9.3 (98.0) 6.2 (98.9) 29.8 (142.2) 44.9 (40.5, 114.2) Rpim (%) 15.7 (55.3) 10.3 (109.0) 3.7 (53.8) 6.3 (40.0) 24.7 (23.9, 59.9) Refinement Rwork (%) 17.9 18.4 21.6 20.2 32.1 Rfree (%) 22.7 23.2 30.7 27.1 35.5 No. of Non-Hydrogen Atoms Protein 2,260 2,301 2,102 2,305 7,730 N-glycans 42 42 28 28 0 Water 79 54 0 2 0 Ligands 6 6 2 5 0 Average B factor (Γ
2) Protein 63 65 108 84 β N-glycans 35 46 102 18 β Water 68 85 β 75 β Ligands 36 47 91 75 66 RMSD from Ideality Bond lengths (Γ
) 0.020 0.016 0.019 0.016 0.004 Bond angles (Β°) 2.050 1.748 1.952 1.796 0.770 Ramachandran Plot Favored (%) 96.8 95.5 96.9 94.9 92.3 Allowed (%) 99.7 100.0 100.0 99.7 99.8 Number of outliers 1 0 0 1 2 PDB code 5FWS 5FWT 5FWU 5FWV 5FWW " TABLE |
|
1466 1470 RMSD evidence " KRM1ECD KRM1ECD KRM1ECD KRM1ECD LRP6PE3PE4-DKKCRD2-KRM1ECD Crystal form I I II III I X-ray source Diamond i04 Diamond i03 Diamond i03 Diamond i04 Diamond i04 Wavelength (Γ
) 0.9793 0.9700 0.9700 0.9795 0.9795 Space group P3121 P3121 P43 P41212 C2221 Unit cell a/Ξ± (Γ
/Β°) 50.9/90 50.5/90 65.8/90 67.8/90 86.9/90 b/Ξ² (Γ
/Β°) 50.9/90 50.5/90 65.8/90 67.8/90 100.1/90 c/Ξ³ (Γ
/Β°) 188.4/120 187.4/120 75.0/90 198.2/90 270.7/90 Wilson B factor (Γ
2) 31 41 76 77 NA Resolution range (Γ
) 47.10β1.90 (1.95β1.90) 62.47β2.10 (2.16β2.10) 75.00β2.80 (2.99β2.80) 67.80β3.20 (3.42β3.20) 67.68β3.50 (7.16β6.40, 3.92β3.50) Unique reflections 23,300 (1,524) 17,089 (1,428) 7,964 (1,448) 8,171 (1,343) 8,070 (723, 645) Average multiplicity 9.1 (9.2) 5.2 (5.3) 3.7 (3.7) 22.7 (12.6) 3.8 (3.5, 4.4) Completeness (%) 99.8 (98.5) 100 (100) 99.8 (100) 98.8 (93.4) 51.6 (98.5, 14.1) <I/ΟI> 11.4 (1.7) 12.0 (1.7) 14.9 (1.5) 13.1 (1.9) 4.6 (4.1, 2.2) Rmerge (%) 14.8 (158.3) 9.3 (98.0) 6.2 (98.9) 29.8 (142.2) 44.9 (40.5, 114.2) Rpim (%) 15.7 (55.3) 10.3 (109.0) 3.7 (53.8) 6.3 (40.0) 24.7 (23.9, 59.9) Refinement Rwork (%) 17.9 18.4 21.6 20.2 32.1 Rfree (%) 22.7 23.2 30.7 27.1 35.5 No. of Non-Hydrogen Atoms Protein 2,260 2,301 2,102 2,305 7,730 N-glycans 42 42 28 28 0 Water 79 54 0 2 0 Ligands 6 6 2 5 0 Average B factor (Γ
2) Protein 63 65 108 84 β N-glycans 35 46 102 18 β Water 68 85 β 75 β Ligands 36 47 91 75 66 RMSD from Ideality Bond lengths (Γ
) 0.020 0.016 0.019 0.016 0.004 Bond angles (Β°) 2.050 1.748 1.952 1.796 0.770 Ramachandran Plot Favored (%) 96.8 95.5 96.9 94.9 92.3 Allowed (%) 99.7 100.0 100.0 99.7 99.8 Number of outliers 1 0 0 1 2 PDB code 5FWS 5FWT 5FWU 5FWV 5FWW " TABLE |
|
99 115 diffraction data evidence An additional shell given for the ternary complex corresponds to the last shell with near-complete diffraction data. TABLE |
|
|
