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http://purl.uniprot.org/citations/11713476http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11713476http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11713476http://www.w3.org/2000/01/rdf-schema#comment"The multifunctional protein beta-catenin is important for cell adhesion, because it binds cadherins, and the Wnt signal transduction pathway, where it interacts with the Adenomatous polyposis coli (APC) protein and TCF/Lef family transcription factors. Mutations in APC or in beta-catenin are estimated to trigger formation of over 90% of all colon cancers. In colonic epithelia, these mutations produce elevated levels of Tcf4-beta-catenin, which stimulates a transcriptional response that initiates polyp formation and eventually malignant growth. Thus, disruption of the Tcf4-beta-catenin interaction may be an attractive goal for therapeutic intervention. Here we describe the crystal structure of a human Tcf4-beta-catenin complex and compare it with recent structures of beta-catenin in complex with Xenopus Tcf3 (XTcf3) and mammalian E-cadherin. The structure reveals anticipated similarities with the closely related XTcf3 complex but unexpectedly lacks one component observed in the XTcf3 structure."xsd:string
http://purl.uniprot.org/citations/11713476http://purl.org/dc/terms/identifier"doi:10.1038/nsb720"xsd:string
http://purl.uniprot.org/citations/11713476http://purl.org/dc/terms/identifier"doi:10.1038/nsb720"xsd:string
http://purl.uniprot.org/citations/11713476http://purl.uniprot.org/core/author"Eck M.J."xsd:string
http://purl.uniprot.org/citations/11713476http://purl.uniprot.org/core/author"Eck M.J."xsd:string
http://purl.uniprot.org/citations/11713476http://purl.uniprot.org/core/author"Poy F."xsd:string
http://purl.uniprot.org/citations/11713476http://purl.uniprot.org/core/author"Poy F."xsd:string
http://purl.uniprot.org/citations/11713476http://purl.uniprot.org/core/author"Shivdasani R.A."xsd:string
http://purl.uniprot.org/citations/11713476http://purl.uniprot.org/core/author"Shivdasani R.A."xsd:string
http://purl.uniprot.org/citations/11713476http://purl.uniprot.org/core/author"Lepourcelet M."xsd:string
http://purl.uniprot.org/citations/11713476http://purl.uniprot.org/core/author"Lepourcelet M."xsd:string
http://purl.uniprot.org/citations/11713476http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11713476http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11713476http://purl.uniprot.org/core/name"Nat. Struct. Biol."xsd:string
http://purl.uniprot.org/citations/11713476http://purl.uniprot.org/core/name"Nat. Struct. Biol."xsd:string
http://purl.uniprot.org/citations/11713476http://purl.uniprot.org/core/pages"1053-1057"xsd:string
http://purl.uniprot.org/citations/11713476http://purl.uniprot.org/core/pages"1053-1057"xsd:string
http://purl.uniprot.org/citations/11713476http://purl.uniprot.org/core/title"Structure of a human Tcf4-beta-catenin complex."xsd:string
http://purl.uniprot.org/citations/11713476http://purl.uniprot.org/core/title"Structure of a human Tcf4-beta-catenin complex."xsd:string
http://purl.uniprot.org/citations/11713476http://purl.uniprot.org/core/volume"8"xsd:string
http://purl.uniprot.org/citations/11713476http://purl.uniprot.org/core/volume"8"xsd:string
http://purl.uniprot.org/citations/11713476http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11713476
http://purl.uniprot.org/citations/11713476http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11713476