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XB-ART-47293
Structure 2013 Jul 02;217:1235-42. doi: 10.1016/j.str.2013.05.006.
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structural Studies of Wnts and identification of an LRP6 binding site.

Chu ML , Ahn VE , Choi HJ , Daniels DL , Nusse R , Weis WI .


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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.

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Species referenced: Xenopus
Genes referenced: ctnnb1 lrp5 lrp6 wnt3a wnt8a

References [+] :
Adams, PHENIX: building new software for automated crystallographic structure determination. 2002, Pubmed