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http://purl.uniprot.org/citations/8836101http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8836101http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8836101http://www.w3.org/2000/01/rdf-schema#comment"Cyclin-dependent kinases (CDKs), which play a key role in cell cycle control, are activated by the CDK activating kinase (CAK), which activates cyclin-bound CDKs by phosphorylation at a specific threonine residue. Vertebrate CAK contains two key components: a kinase subunit with homology to its substrate CDKs and a regulatory subunit with homology to cyclins. We have determined the X-ray crystal structure of the regulatory subunit of CAK, cyclin H, at 2.6 A resolution. Cyclin H contains two alpha-helical core domains with a fold similar to that of cyclin A, a regulatory subunit of CAK substrate CDK2, and of TFIIB, a transcription factor. Outside of the core domains, the N- and C-terminal regions of the three structures are completely different. The conformational differences between cyclin H and A structures may reflect functional differences between the two cyclins."xsd:string
http://purl.uniprot.org/citations/8836101http://purl.org/dc/terms/identifier"doi:10.1038/nsb1096-849"xsd:string
http://purl.uniprot.org/citations/8836101http://purl.org/dc/terms/identifier"doi:10.1038/nsb1096-849"xsd:string
http://purl.uniprot.org/citations/8836101http://purl.uniprot.org/core/author"Kim K.K."xsd:string
http://purl.uniprot.org/citations/8836101http://purl.uniprot.org/core/author"Kim K.K."xsd:string
http://purl.uniprot.org/citations/8836101http://purl.uniprot.org/core/author"Kim S.-H."xsd:string
http://purl.uniprot.org/citations/8836101http://purl.uniprot.org/core/author"Kim S.-H."xsd:string
http://purl.uniprot.org/citations/8836101http://purl.uniprot.org/core/author"Morgan D.O."xsd:string
http://purl.uniprot.org/citations/8836101http://purl.uniprot.org/core/author"Morgan D.O."xsd:string
http://purl.uniprot.org/citations/8836101http://purl.uniprot.org/core/author"Chamberlin H.M."xsd:string
http://purl.uniprot.org/citations/8836101http://purl.uniprot.org/core/author"Chamberlin H.M."xsd:string
http://purl.uniprot.org/citations/8836101http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8836101http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8836101http://purl.uniprot.org/core/name"Nat. Struct. Biol."xsd:string
http://purl.uniprot.org/citations/8836101http://purl.uniprot.org/core/name"Nat. Struct. Biol."xsd:string
http://purl.uniprot.org/citations/8836101http://purl.uniprot.org/core/pages"849-855"xsd:string
http://purl.uniprot.org/citations/8836101http://purl.uniprot.org/core/pages"849-855"xsd:string
http://purl.uniprot.org/citations/8836101http://purl.uniprot.org/core/title"Three-dimensional structure of human cyclin H, a positive regulator of the CDK-activating kinase."xsd:string
http://purl.uniprot.org/citations/8836101http://purl.uniprot.org/core/title"Three-dimensional structure of human cyclin H, a positive regulator of the CDK-activating kinase."xsd:string
http://purl.uniprot.org/citations/8836101http://purl.uniprot.org/core/volume"3"xsd:string
http://purl.uniprot.org/citations/8836101http://purl.uniprot.org/core/volume"3"xsd:string
http://purl.uniprot.org/citations/8836101http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8836101
http://purl.uniprot.org/citations/8836101http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8836101