@article {387,
	title = {structural Studies of Wnts and identification of an LRP6 binding site.},
	journal = {Structure (London, England : 1993)},
	volume = {21},
	year = {2013},
	month = {2013 Jul 2},
	pages = {1235-42},
	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~{\r 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 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.},
	issn = {0969-2126},
	doi = {10.1016/j.str.2013.05.006},
	url = {http://linkinghub.elsevier.com/retrieve/pii/S0969-2126(13)00164-0},
	author = {Chu, ML and Ahn, VE and Choi, HJ and Daniels, DL and Nusse, R and Weis, WI}
}
