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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2001-5-11
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pubmed:abstractText |
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.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenomatous Polyposis Coli Protein,
http://linkedlifedata.com/resource/pubmed/chemical/CTNNB1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cadherins,
http://linkedlifedata.com/resource/pubmed/chemical/Casein Kinase II,
http://linkedlifedata.com/resource/pubmed/chemical/Catnb protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Desmoplakins,
http://linkedlifedata.com/resource/pubmed/chemical/HMGB Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/TCF Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/TCF7L1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Tcf7l1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor 7-Like 1...,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/beta Catenin
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
4
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pubmed:volume |
105
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
391-402
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:11348595-Adenomatous Polyposis Coli Protein,
pubmed-meshheading:11348595-Adherens Junctions,
pubmed-meshheading:11348595-Amino Acid Motifs,
pubmed-meshheading:11348595-Amino Acid Sequence,
pubmed-meshheading:11348595-Animals,
pubmed-meshheading:11348595-Binding Sites,
pubmed-meshheading:11348595-Cadherins,
pubmed-meshheading:11348595-Casein Kinase II,
pubmed-meshheading:11348595-Crystallography, X-Ray,
pubmed-meshheading:11348595-Cytoskeletal Proteins,
pubmed-meshheading:11348595-Desmoplakins,
pubmed-meshheading:11348595-HMGB Proteins,
pubmed-meshheading:11348595-Humans,
pubmed-meshheading:11348595-Ligands,
pubmed-meshheading:11348595-Mice,
pubmed-meshheading:11348595-Models, Molecular,
pubmed-meshheading:11348595-Molecular Sequence Data,
pubmed-meshheading:11348595-Phosphorylation,
pubmed-meshheading:11348595-Protein Conformation,
pubmed-meshheading:11348595-Protein Structure, Secondary,
pubmed-meshheading:11348595-Protein Structure, Tertiary,
pubmed-meshheading:11348595-Protein-Serine-Threonine Kinases,
pubmed-meshheading:11348595-Recombinant Proteins,
pubmed-meshheading:11348595-Sequence Alignment,
pubmed-meshheading:11348595-TCF Transcription Factors,
pubmed-meshheading:11348595-Trans-Activators,
pubmed-meshheading:11348595-Transcription Factor 7-Like 1 Protein,
pubmed-meshheading:11348595-Transcription Factors,
pubmed-meshheading:11348595-beta Catenin
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pubmed:year |
2001
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pubmed:articleTitle |
The structure of the beta-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by beta-catenin.
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pubmed:affiliation |
Departments of Structural Biology and Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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