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http://purl.uniprot.org/citations/11348595http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11348595http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11348595http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/11348595http://purl.org/dc/terms/identifier"doi:10.1016/s0092-8674(01)00330-0"xsd:string
http://purl.uniprot.org/citations/11348595http://purl.org/dc/terms/identifier"doi:10.1016/s0092-8674(01)00330-0"xsd:string
http://purl.uniprot.org/citations/11348595http://purl.uniprot.org/core/author"Weis W.I."xsd:string
http://purl.uniprot.org/citations/11348595http://purl.uniprot.org/core/author"Weis W.I."xsd:string
http://purl.uniprot.org/citations/11348595http://purl.uniprot.org/core/author"Huber A.H."xsd:string
http://purl.uniprot.org/citations/11348595http://purl.uniprot.org/core/author"Huber A.H."xsd:string
http://purl.uniprot.org/citations/11348595http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11348595http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11348595http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/11348595http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/11348595http://purl.uniprot.org/core/pages"391-402"xsd:string
http://purl.uniprot.org/citations/11348595http://purl.uniprot.org/core/pages"391-402"xsd:string
http://purl.uniprot.org/citations/11348595http://purl.uniprot.org/core/title"The structure of the beta-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by beta-catenin."xsd:string
http://purl.uniprot.org/citations/11348595http://purl.uniprot.org/core/title"The structure of the beta-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by beta-catenin."xsd:string
http://purl.uniprot.org/citations/11348595http://purl.uniprot.org/core/volume"105"xsd:string
http://purl.uniprot.org/citations/11348595http://purl.uniprot.org/core/volume"105"xsd:string
http://purl.uniprot.org/citations/11348595http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11348595
http://purl.uniprot.org/citations/11348595http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11348595
http://purl.uniprot.org/citations/11348595http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11348595
http://purl.uniprot.org/citations/11348595http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11348595
http://purl.uniprot.org/uniprot/P09803http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/11348595
http://purl.uniprot.org/uniprot/Q02248http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/11348595