Journal
EMBO JOURNAL
Volume 20, Issue 22, Pages 6203-6212Publisher
OXFORD UNIV PRESS
DOI: 10.1093/emboj/20.22.6203
Keywords
adenomatous polyposis coli; beta-catenin; crystal structure; Wnt signaling
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Funding
- NIGMS NIH HHS [R01 GM056169, GM56169] Funding Source: Medline
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The adenomatous polyposis coli (APC) tumor suppressor protein plays a critical role in regulating cellular levels of the oncogene product beta -catenin. APC binds to beta -catenin through a series of homologous 15 and 20 amino acid repeats. We have determined the crystal structure of a 15 amino acid beta -catenin binding repeat from APC bound to the armadillo repeat region of beta -catenin. Although it lacks significant sequence homology, the N-terminal half of the repeat binds in a manner similar to portions of E-cadherin and XTcf3, but the remaining interactions are unique to APC. We discuss the implications of this new structure for the design of therapeutics, and present evidence from structural, biochemical and sequence data, which suggest that the 20 amino acid repeats can adopt two modes of binding to beta -catenin.
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