4krr

Publication Abstract from PubMed

Wnts are secreted growth factors that have critical roles in cell fate determination and stem cell renewal. The Wnt/beta-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 A 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 beta 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.

Structural Studies of Wnts and Identification of an LRP6 Binding Site.,Chu ML, Ahn VE, Choi HJ, Daniels DL, Nusse R, Weis WI Structure. 2013 Jul 2;21(7):1235-42. doi: 10.1016/j.str.2013.05.006. Epub 2013, Jun 20. PMID:23791946^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.