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http://purl.uniprot.org/citations/8756328http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8756328http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8756328http://www.w3.org/2000/01/rdf-schema#comment"Cyclin-dependent kinase (CDK)-cyclin complexes require phosphorylation on the CDK subunit for full activation of their Ser/Thr protein kinase activity. The crystal structure of the phosphorylated CDK2-CyclinA-ATP gamma S complex has been determined at 2.6 A resolution. The phosphate group, which is on the regulatory T-loop of CDK2, is mostly buried, its charge being neutralized by three Arg side chains. The arginines help extend the influence of the phosphate group through a network of hydrogen bonds to both CDK2 and cyclinA. Comparison with the unphosphorylated CDK2-CyclinA complex shows that the T-loop moves by as much as 7 A, and this affects the putative substrate binding site as well as resulting in additional CDK2-CyclinA contacts. The phosphate group thus acts as a major organizing centre in the CDK2-CyclinA complex."xsd:string
http://purl.uniprot.org/citations/8756328http://purl.org/dc/terms/identifier"doi:10.1038/nsb0896-696"xsd:string
http://purl.uniprot.org/citations/8756328http://purl.org/dc/terms/identifier"doi:10.1038/nsb0896-696"xsd:string
http://purl.uniprot.org/citations/8756328http://purl.uniprot.org/core/author"Jeffrey P.D."xsd:string
http://purl.uniprot.org/citations/8756328http://purl.uniprot.org/core/author"Jeffrey P.D."xsd:string
http://purl.uniprot.org/citations/8756328http://purl.uniprot.org/core/author"Pavletich N.P."xsd:string
http://purl.uniprot.org/citations/8756328http://purl.uniprot.org/core/author"Pavletich N.P."xsd:string
http://purl.uniprot.org/citations/8756328http://purl.uniprot.org/core/author"Russo A.A."xsd:string
http://purl.uniprot.org/citations/8756328http://purl.uniprot.org/core/author"Russo A.A."xsd:string
http://purl.uniprot.org/citations/8756328http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8756328http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8756328http://purl.uniprot.org/core/name"Nat. Struct. Biol."xsd:string
http://purl.uniprot.org/citations/8756328http://purl.uniprot.org/core/name"Nat. Struct. Biol."xsd:string
http://purl.uniprot.org/citations/8756328http://purl.uniprot.org/core/pages"696-700"xsd:string
http://purl.uniprot.org/citations/8756328http://purl.uniprot.org/core/pages"696-700"xsd:string
http://purl.uniprot.org/citations/8756328http://purl.uniprot.org/core/title"Structural basis of cyclin-dependent kinase activation by phosphorylation."xsd:string
http://purl.uniprot.org/citations/8756328http://purl.uniprot.org/core/title"Structural basis of cyclin-dependent kinase activation by phosphorylation."xsd:string
http://purl.uniprot.org/citations/8756328http://purl.uniprot.org/core/volume"3"xsd:string
http://purl.uniprot.org/citations/8756328http://purl.uniprot.org/core/volume"3"xsd:string
http://purl.uniprot.org/citations/8756328http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8756328
http://purl.uniprot.org/citations/8756328http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8756328
http://purl.uniprot.org/citations/8756328http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8756328
http://purl.uniprot.org/citations/8756328http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8756328