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http://purl.uniprot.org/citations/22081014http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22081014http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22081014http://www.w3.org/2000/01/rdf-schema#comment"Members of the novel SH2-containing protein (NSP) and Crk-associated substrate (Cas) protein families form multidomain signaling platforms that mediate cell migration and invasion through a collection of distinct signaling motifs. Members of each family interact via their respective C-terminal domains, but the mechanism of this association has remained enigmatic. Here we present the crystal structures of the C-terminal domain from the NSP protein BCAR3 and the complex of NSP3 with p130Cas. BCAR3 adopts the Cdc25-homology fold of Ras GTPase exchange factors, but it has a 'closed' conformation incapable of enzymatic activity. The structure of the NSP3-p130Cas complex reveals that this closed conformation is instrumental for interaction of NSP proteins with a focal adhesion-targeting domain present in Cas proteins. This enzyme-to-adaptor conversion enables high-affinity, yet promiscuous, interactions between NSP and Cas proteins and represents an unprecedented mechanistic paradigm linking cellular signaling networks."xsd:string
http://purl.uniprot.org/citations/22081014http://purl.org/dc/terms/identifier"doi:10.1038/nsmb.2152"xsd:string
http://purl.uniprot.org/citations/22081014http://purl.org/dc/terms/identifier"doi:10.1038/nsmb.2152"xsd:string
http://purl.uniprot.org/citations/22081014http://purl.uniprot.org/core/author"Lee J.J."xsd:string
http://purl.uniprot.org/citations/22081014http://purl.uniprot.org/core/author"Lee J.J."xsd:string
http://purl.uniprot.org/citations/22081014http://purl.uniprot.org/core/author"Robinson H."xsd:string
http://purl.uniprot.org/citations/22081014http://purl.uniprot.org/core/author"Robinson H."xsd:string
http://purl.uniprot.org/citations/22081014http://purl.uniprot.org/core/author"Mace P.D."xsd:string
http://purl.uniprot.org/citations/22081014http://purl.uniprot.org/core/author"Mace P.D."xsd:string
http://purl.uniprot.org/citations/22081014http://purl.uniprot.org/core/author"Dobaczewska M.K."xsd:string
http://purl.uniprot.org/citations/22081014http://purl.uniprot.org/core/author"Dobaczewska M.K."xsd:string
http://purl.uniprot.org/citations/22081014http://purl.uniprot.org/core/author"Pasquale E.B."xsd:string
http://purl.uniprot.org/citations/22081014http://purl.uniprot.org/core/author"Pasquale E.B."xsd:string
http://purl.uniprot.org/citations/22081014http://purl.uniprot.org/core/author"Riedl S.J."xsd:string
http://purl.uniprot.org/citations/22081014http://purl.uniprot.org/core/author"Riedl S.J."xsd:string
http://purl.uniprot.org/citations/22081014http://purl.uniprot.org/core/author"Wallez Y."xsd:string
http://purl.uniprot.org/citations/22081014http://purl.uniprot.org/core/author"Wallez Y."xsd:string
http://purl.uniprot.org/citations/22081014http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/22081014http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/22081014http://purl.uniprot.org/core/name"Nat. Struct. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/22081014http://purl.uniprot.org/core/name"Nat. Struct. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/22081014http://purl.uniprot.org/core/pages"1381-1387"xsd:string
http://purl.uniprot.org/citations/22081014http://purl.uniprot.org/core/pages"1381-1387"xsd:string