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XB-ART-47293
Structure. July 2, 2013; 21 (7): 1235-42.

structural Studies of Wnts and identification of an LRP6 binding site.

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


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 ID: 23791946
PMC ID: PMC3731992
Article link: Structure.
Grant support: AG33596 NIA NIH HHS , AG39420 NIA NIH HHS , R01 AG039420 NIA NIH HHS , R21 AG033596 NIA NIH HHS

Genes referenced: lrp5 lrp6 wnt3a wnt8a
Antibodies referenced:

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