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http://purl.uniprot.org/citations/22888118http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22888118http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22888118http://www.w3.org/2000/01/rdf-schema#comment"Through their ubiquitin ligase activity, Cbl-family proteins suppress signalling mediated by protein-tyrosine kinases (PTKs), but can also function as adaptor proteins to positively regulate signalling. The tyrosine kinase binding (TKB) domain of this family is critical for binding with tyrosine-phosphorylated target proteins. Here, we analysed the crystal structure of the TKB domain of Cbl-c/Cbl-3 (Cbl-c TKB), which is a distinct member of the mammalian Cbl-family. In comparison with Cbl TKB, Cbl-c TKB showed restricted structural flexibility upon phosphopeptide binding. A mutation in Cbl-c TKB augmenting this flexibility enhanced its binding to target phosphoproteins. These results suggest that proteins, post-translational modifications or mutations that alter structural flexibility of the TKB domain of Cbl-family proteins could regulate their binding to target phosphoproteins and thereby, affect PTK-mediated signalling."xsd:string
http://purl.uniprot.org/citations/22888118http://purl.org/dc/terms/identifier"doi:10.1093/jb/mvs085"xsd:string
http://purl.uniprot.org/citations/22888118http://purl.org/dc/terms/identifier"doi:10.1093/jb/mvs085"xsd:string
http://purl.uniprot.org/citations/22888118http://purl.uniprot.org/core/author"Kim M."xsd:string
http://purl.uniprot.org/citations/22888118http://purl.uniprot.org/core/author"Kim M."xsd:string
http://purl.uniprot.org/citations/22888118http://purl.uniprot.org/core/author"Nakagawa A."xsd:string
http://purl.uniprot.org/citations/22888118http://purl.uniprot.org/core/author"Nakagawa A."xsd:string
http://purl.uniprot.org/citations/22888118http://purl.uniprot.org/core/author"Suzuki M."xsd:string
http://purl.uniprot.org/citations/22888118http://purl.uniprot.org/core/author"Suzuki M."xsd:string
http://purl.uniprot.org/citations/22888118http://purl.uniprot.org/core/author"Yamamoto T."xsd:string
http://purl.uniprot.org/citations/22888118http://purl.uniprot.org/core/author"Yamamoto T."xsd:string
http://purl.uniprot.org/citations/22888118http://purl.uniprot.org/core/author"Yamashita E."xsd:string
http://purl.uniprot.org/citations/22888118http://purl.uniprot.org/core/author"Yamashita E."xsd:string
http://purl.uniprot.org/citations/22888118http://purl.uniprot.org/core/author"Yamanashi Y."xsd:string
http://purl.uniprot.org/citations/22888118http://purl.uniprot.org/core/author"Yamanashi Y."xsd:string
http://purl.uniprot.org/citations/22888118http://purl.uniprot.org/core/author"Tezuka T."xsd:string
http://purl.uniprot.org/citations/22888118http://purl.uniprot.org/core/author"Tezuka T."xsd:string
http://purl.uniprot.org/citations/22888118http://purl.uniprot.org/core/author"Takeshita K."xsd:string
http://purl.uniprot.org/citations/22888118http://purl.uniprot.org/core/author"Takeshita K."xsd:string
http://purl.uniprot.org/citations/22888118http://purl.uniprot.org/core/author"Isozaki Y."xsd:string
http://purl.uniprot.org/citations/22888118http://purl.uniprot.org/core/author"Isozaki Y."xsd:string
http://purl.uniprot.org/citations/22888118http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22888118http://purl.uniprot.org/core/date"2012"xsd:gYear