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http://purl.uniprot.org/citations/17052462http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17052462http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17052462http://www.w3.org/2000/01/rdf-schema#comment"The canonical Wnt pathway plays critical roles in embryonic development, stem cell growth, and tumorigenesis. Stimulation of the Wnt pathway leads to the association of beta-catenin with Tcf and BCL9 in the nucleus, resulting in the transactivation of Wnt target genes. We have determined the crystal structure of a beta-catenin/BCL9/Tcf-4 triple complex at 2.6 A resolution. Our studies reveal that the beta-catenin binding site of BCL9 is distinct from that of most other beta-catenin partners and forms a good target for developing drugs that block canonical Wnt/beta-catenin signaling. The BCL9 beta-catenin binding domain (CBD) forms an alpha helix that binds to the first armadillo repeat of beta-catenin, which can be mutated to prevent beta-catenin binding to BCL9 without affecting cadherin or alpha-catenin binding. We also demonstrate that beta-catenin Y142 phosphorylation, which has been proposed to regulate BCL9-2 binding, does not directly affect the interaction of beta-catenin with either BCL9 or BCL9-2."xsd:string
http://purl.uniprot.org/citations/17052462http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2006.09.001"xsd:string
http://purl.uniprot.org/citations/17052462http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2006.09.001"xsd:string
http://purl.uniprot.org/citations/17052462http://purl.uniprot.org/core/author"Cho U.S."xsd:string
http://purl.uniprot.org/citations/17052462http://purl.uniprot.org/core/author"Cho U.S."xsd:string
http://purl.uniprot.org/citations/17052462http://purl.uniprot.org/core/author"Xu W."xsd:string
http://purl.uniprot.org/citations/17052462http://purl.uniprot.org/core/author"Xu W."xsd:string
http://purl.uniprot.org/citations/17052462http://purl.uniprot.org/core/author"Kimelman D."xsd:string
http://purl.uniprot.org/citations/17052462http://purl.uniprot.org/core/author"Kimelman D."xsd:string
http://purl.uniprot.org/citations/17052462http://purl.uniprot.org/core/author"Hinds T.R."xsd:string
http://purl.uniprot.org/citations/17052462http://purl.uniprot.org/core/author"Hinds T.R."xsd:string
http://purl.uniprot.org/citations/17052462http://purl.uniprot.org/core/author"Dahlberg C.L."xsd:string
http://purl.uniprot.org/citations/17052462http://purl.uniprot.org/core/author"Dahlberg C.L."xsd:string
http://purl.uniprot.org/citations/17052462http://purl.uniprot.org/core/author"Sampietro J."xsd:string
http://purl.uniprot.org/citations/17052462http://purl.uniprot.org/core/author"Sampietro J."xsd:string
http://purl.uniprot.org/citations/17052462http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17052462http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17052462http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/17052462http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/17052462http://purl.uniprot.org/core/pages"293-300"xsd:string
http://purl.uniprot.org/citations/17052462http://purl.uniprot.org/core/pages"293-300"xsd:string
http://purl.uniprot.org/citations/17052462http://purl.uniprot.org/core/title"Crystal structure of a beta-catenin/BCL9/Tcf4 complex."xsd:string
http://purl.uniprot.org/citations/17052462http://purl.uniprot.org/core/title"Crystal structure of a beta-catenin/BCL9/Tcf4 complex."xsd:string