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http://purl.uniprot.org/citations/15130468http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15130468http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15130468http://www.w3.org/2000/01/rdf-schema#comment"Uridine-cytidine kinase (UCK) catalyzes the phosphorylation of uridine and cytidine and activates pharmacological ribonucleoside analogs. Here we present the crystal structures of human UCK alone and in complexes with a substrate, cytidine, a feedback inhibitor, CTP or UTP, and with phosphorylation products, CMP and ADP, respectively. Free UCK takes an alpha/beta mononucleotide binding fold and exists as a homotetramer with 222 symmetry. Upon inhibitor binding, one loop region was loosened, causing the UCK tetramer to be distorted. Upon cytidine binding, a large induced fit was observed at the uridine/cytidine binding site, which endows UCK with a strict specificity for pyrimidine ribonucleosides. The first UCK structure provided the structural basis for the specificity, catalysis, and regulation of human uridine-cytidine kinase, which give clues for the design of novel antitumor and antiviral ribonucleoside analogs that inhibit RNA synthesis."xsd:string
http://purl.uniprot.org/citations/15130468http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2004.02.038"xsd:string
http://purl.uniprot.org/citations/15130468http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2004.02.038"xsd:string
http://purl.uniprot.org/citations/15130468http://purl.uniprot.org/core/author"Inagaki F."xsd:string
http://purl.uniprot.org/citations/15130468http://purl.uniprot.org/core/author"Inagaki F."xsd:string
http://purl.uniprot.org/citations/15130468http://purl.uniprot.org/core/author"Matsuda A."xsd:string
http://purl.uniprot.org/citations/15130468http://purl.uniprot.org/core/author"Matsuda A."xsd:string
http://purl.uniprot.org/citations/15130468http://purl.uniprot.org/core/author"Fukushima M."xsd:string
http://purl.uniprot.org/citations/15130468http://purl.uniprot.org/core/author"Fukushima M."xsd:string
http://purl.uniprot.org/citations/15130468http://purl.uniprot.org/core/author"Koizumi K."xsd:string
http://purl.uniprot.org/citations/15130468http://purl.uniprot.org/core/author"Koizumi K."xsd:string
http://purl.uniprot.org/citations/15130468http://purl.uniprot.org/core/author"Suzuki N.N."xsd:string
http://purl.uniprot.org/citations/15130468http://purl.uniprot.org/core/author"Suzuki N.N."xsd:string
http://purl.uniprot.org/citations/15130468http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15130468http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15130468http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/15130468http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/15130468http://purl.uniprot.org/core/pages"751-764"xsd:string
http://purl.uniprot.org/citations/15130468http://purl.uniprot.org/core/pages"751-764"xsd:string
http://purl.uniprot.org/citations/15130468http://purl.uniprot.org/core/title"Structural basis for the specificity, catalysis, and regulation of human uridine-cytidine kinase."xsd:string
http://purl.uniprot.org/citations/15130468http://purl.uniprot.org/core/title"Structural basis for the specificity, catalysis, and regulation of human uridine-cytidine kinase."xsd:string
http://purl.uniprot.org/citations/15130468http://purl.uniprot.org/core/volume"12"xsd:string
http://purl.uniprot.org/citations/15130468http://purl.uniprot.org/core/volume"12"xsd:string