4KRR
Crystal structure of Drosophila WntD N-terminal domain-linker (residues 31-240)
Summary for 4KRR
| Entry DOI | 10.2210/pdb4krr/pdb |
| Descriptor | Wnt inhibitor of Dorsal protein, GLYCEROL, SODIUM ION, ... (4 entities in total) |
| Functional Keywords | wntd, uncomplexed wnt, n-terminal domain, linker, wnt, growth factor, wnt signaling, extracellular, signaling protein |
| Biological source | Drosophila melanogaster (Fruit fly) |
| Total number of polymer chains | 1 |
| Total formula weight | 24920.77 |
| Authors | Chu, M.L.-H.,Choi, H.-J.,Ahn, V.E.,Daniels, D.L.,Nusse, R.,Weis, W.I. (deposition date: 2013-05-16, release date: 2013-07-10, Last modification date: 2024-10-30) |
| Primary citation | Chu, M.L.,Ahn, V.E.,Choi, H.J.,Daniels, D.L.,Nusse, R.,Weis, W.I. Structural Studies of Wnts and Identification of an LRP6 Binding Site. Structure, 21:1235-1242, 2013 Cited by PubMed Abstract: Wnts are secreted growth factors that have critical roles in cell fate determination and stem cell renewal. The Wnt/β-catenin pathway is initiated by binding of a Wnt protein to a Frizzled (Fzd) receptor and a coreceptor, LDL receptor-related protein 5 or 6 (LRP5/6). We report the 2.1 Å resolution crystal structure of a Drosophila WntD fragment encompassing the N-terminal domain and the linker that connects it to the C-terminal domain. Differences in the structures of WntD and Xenopus Wnt8, including the positions of a receptor-binding β hairpin and a large solvent-filled cavity in the helical core, indicate conformational plasticity in the N-terminal domain that may be important for Wnt-Frizzled specificity. Structure-based mutational analysis of mouse Wnt3a shows that the linker between the N- and C-terminal domains is required for LRP6 binding. These findings provide important insights into Wnt function and evolution. PubMed: 23791946DOI: 10.1016/j.str.2013.05.006 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.124 Å) |
Structure validation
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