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1i7w
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(New page: 200px<br /><applet load="1i7w" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i7w, resolution 2.00Å" /> '''BETA-CATENIN/PHOSPHO...)
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Revision as of 15:00, 20 November 2007
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BETA-CATENIN/PHOSPHORYLATED E-CADHERIN COMPLEX
Overview
As a component of adherens junctions and the Wnt signaling pathway, beta-catenin binds cadherins, Tcf family transcription factors, and the, tumor suppressor APC. We have determined the crystal structures of both, unphosphorylated and phosphorylated E-cadherin cytoplasmic domain, complexed with the arm repeat region of beta-catenin. The interaction, spans all 12 arm repeats, and features quasi-independent binding regions, that include helices which interact with both ends of the arm repeat, domain and an extended stretch of 14 residues which closely resembles a, portion of XTcf-3. Phosphorylation of E-cadherin results in interactions, with a hydrophobic patch of beta-catenin that mimics the binding of an, amphipathic XTcf-3 helix. APC contains sequences homologous to the, phosphorylated region of cadherin, and is likely to bind similarly.
About this Structure
1I7W is a Protein complex structure of sequences from Mus musculus with ZN and CL as ligands. Full crystallographic information is available from OCA.
Reference
The structure of the beta-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by beta-catenin., Huber AH, Weis WI, Cell. 2001 May 4;105(3):391-402. PMID:11348595
Page seeded by OCA on Tue Nov 20 17:08:08 2007
