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http://purl.uniprot.org/citations/15851033http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15851033http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15851033http://www.w3.org/2000/01/rdf-schema#comment"In eukaryotic cells, the SH2 and PTB domains mediate protein-protein interactions by recognizing phosphotyrosine residues on target proteins. Here we make the unexpected finding that the C2 domain of PKCdelta directly binds to phosphotyrosine peptides in a sequence-specific manner. We provide evidence that this domain mediates PKCdelta interaction with a Src binding glycoprotein, CDCP1. The crystal structure of the PKCdelta C2 domain in complex with an optimal phosphopeptide reveals a new mode of phosphotyrosine binding in which the phosphotyrosine moiety forms a ring-stacking interaction with a histidine residue of the C2 domain. This is also the first example of a protein Ser/Thr kinase containing a domain that binds phosphotyrosine."xsd:string
http://purl.uniprot.org/citations/15851033http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2005.02.019"xsd:string
http://purl.uniprot.org/citations/15851033http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2005.02.019"xsd:string
http://purl.uniprot.org/citations/15851033http://purl.uniprot.org/core/author"Cantley L.C."xsd:string
http://purl.uniprot.org/citations/15851033http://purl.uniprot.org/core/author"Cantley L.C."xsd:string
http://purl.uniprot.org/citations/15851033http://purl.uniprot.org/core/author"Wu N."xsd:string
http://purl.uniprot.org/citations/15851033http://purl.uniprot.org/core/author"Wu N."xsd:string
http://purl.uniprot.org/citations/15851033http://purl.uniprot.org/core/author"Soltoff S.P."xsd:string
http://purl.uniprot.org/citations/15851033http://purl.uniprot.org/core/author"Soltoff S.P."xsd:string
http://purl.uniprot.org/citations/15851033http://purl.uniprot.org/core/author"Benes C.H."xsd:string
http://purl.uniprot.org/citations/15851033http://purl.uniprot.org/core/author"Benes C.H."xsd:string
http://purl.uniprot.org/citations/15851033http://purl.uniprot.org/core/author"Dharia T."xsd:string
http://purl.uniprot.org/citations/15851033http://purl.uniprot.org/core/author"Dharia T."xsd:string
http://purl.uniprot.org/citations/15851033http://purl.uniprot.org/core/author"Elia A.E.H."xsd:string
http://purl.uniprot.org/citations/15851033http://purl.uniprot.org/core/author"Elia A.E.H."xsd:string
http://purl.uniprot.org/citations/15851033http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15851033http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15851033http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/15851033http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/15851033http://purl.uniprot.org/core/pages"271-280"xsd:string
http://purl.uniprot.org/citations/15851033http://purl.uniprot.org/core/pages"271-280"xsd:string
http://purl.uniprot.org/citations/15851033http://purl.uniprot.org/core/title"The C2 domain of PKCdelta is a phosphotyrosine binding domain."xsd:string
http://purl.uniprot.org/citations/15851033http://purl.uniprot.org/core/title"The C2 domain of PKCdelta is a phosphotyrosine binding domain."xsd:string