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http://purl.uniprot.org/citations/17512407http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17512407http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17512407http://www.w3.org/2000/01/rdf-schema#comment"ZAP-70, a cytoplasmic tyrosine kinase required for T cell antigen receptor signaling, is controlled by a regulatory segment that includes a tandem SH2 unit responsible for binding to immunoreceptor tyrosine-based activation motifs (ITAMs). The crystal structure of autoinhibited ZAP-70 reveals that the inactive kinase domain adopts a conformation similar to that of cyclin-dependent kinases and Src kinases. The autoinhibitory mechanism of ZAP-70 is, however, distinct and involves interactions between the regulatory segment and the hinge region of the kinase domain that reduce its flexibility. Two tyrosine residues in the SH2-kinase linker that activate ZAP-70 when phosphorylated are involved in aromatic-aromatic interactions that connect the linker to the kinase domain. These interactions are inconsistent with ITAM binding, suggesting that destabilization of this autoinhibited ZAP-70 conformation is the first step in kinase activation."xsd:string
http://purl.uniprot.org/citations/17512407http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2007.03.039"xsd:string
http://purl.uniprot.org/citations/17512407http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2007.03.039"xsd:string
http://purl.uniprot.org/citations/17512407http://purl.uniprot.org/core/author"Kuriyan J."xsd:string
http://purl.uniprot.org/citations/17512407http://purl.uniprot.org/core/author"Kuriyan J."xsd:string
http://purl.uniprot.org/citations/17512407http://purl.uniprot.org/core/author"Cao X."xsd:string
http://purl.uniprot.org/citations/17512407http://purl.uniprot.org/core/author"Cao X."xsd:string
http://purl.uniprot.org/citations/17512407http://purl.uniprot.org/core/author"Weiss A."xsd:string
http://purl.uniprot.org/citations/17512407http://purl.uniprot.org/core/author"Weiss A."xsd:string
http://purl.uniprot.org/citations/17512407http://purl.uniprot.org/core/author"Brdicka T."xsd:string
http://purl.uniprot.org/citations/17512407http://purl.uniprot.org/core/author"Brdicka T."xsd:string
http://purl.uniprot.org/citations/17512407http://purl.uniprot.org/core/author"Kadlecek T.A."xsd:string
http://purl.uniprot.org/citations/17512407http://purl.uniprot.org/core/author"Kadlecek T.A."xsd:string
http://purl.uniprot.org/citations/17512407http://purl.uniprot.org/core/author"Deindl S."xsd:string
http://purl.uniprot.org/citations/17512407http://purl.uniprot.org/core/author"Deindl S."xsd:string
http://purl.uniprot.org/citations/17512407http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17512407http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17512407http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/17512407http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/17512407http://purl.uniprot.org/core/pages"735-746"xsd:string
http://purl.uniprot.org/citations/17512407http://purl.uniprot.org/core/pages"735-746"xsd:string
http://purl.uniprot.org/citations/17512407http://purl.uniprot.org/core/title"Structural basis for the inhibition of tyrosine kinase activity of ZAP-70."xsd:string
http://purl.uniprot.org/citations/17512407http://purl.uniprot.org/core/title"Structural basis for the inhibition of tyrosine kinase activity of ZAP-70."xsd:string