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XB-ART-9767
Cell 2000 Dec 08;1036:885-96. doi: 10.1016/s0092-8674(00)00192-6.
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Crystal structure of a beta-catenin/Tcf complex.

Graham TA, Weaver C, Mao F, Kimelman D, Xu W.


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The Wnt signaling pathway plays critical roles in embryonic development and tumorigenesis. Stimulation of the Wnt pathway results in the accumulation of a nuclear beta-catenin/Tcf complex, activating Wnt target genes. A crystal structure of beta-catenin bound to the beta-catenin binding domain of Tcf3 (Tcf3-CBD) has been determined. The Tcf3-CBD forms an elongated structure with three binding modules that runs antiparallel to beta-catenin along the positively charged groove formed by the armadillo repeats. Structure-based mutagenesis defines three sites in beta-catenin that are critical for binding the Tcf3-CBD and are differentially involved in binding APC, cadherin, and Axin. The structural and mutagenesis data reveal a potential target for molecular drug design studies.

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Species referenced: Xenopus
Genes referenced: tcf3 tcf7l1