http://purl.uniprot.org/citations/8747457 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/8747457 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/8747457 | http://www.w3.org/2000/01/rdf-schema#comment | "BackgroundNucleoside diphosphate (NDP) kinases provide precursors for DNA and RNA synthesis. In mammals, these enzymes are also involved in cell regulations. Human NDP kinase B, product of the human nm23-H2 gene, is both an enzyme and a transcription factor. It activates transcription of the c-myc oncogene independently of its catalytic function, by binding to its promoter DNA. How do the two functions coexist?ResultsRecombinant human NDP kinase B was co-crystallized with GDP. The X-ray structure was solved at 2.0 A resolution by molecular replacement from the homologous Drosophila Awd protein. Both enzymes are homo-hexamers with a characteristic beta alpha beta beta alpha beta fold. GDP binds near the active site His118. The guanine base is in a surface cleft and interacts with the C terminus of another subunit.ConclusionsThe beta alpha beta beta alpha beta fold, also present in the 'palm' domain of Escherichia coli DNA polymerase I and HIV reverse transcriptase, is both a mononucleotide- and a polynucleotide-binding fold. If NDP kinase B binds DNA in the same way as the polymerases, the enzyme must undergo a conformation change in order to carry out gene activation."xsd:string |
http://purl.uniprot.org/citations/8747457 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0969-2126(01)00268-4"xsd:string |
http://purl.uniprot.org/citations/8747457 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0969-2126(01)00268-4"xsd:string |
http://purl.uniprot.org/citations/8747457 | http://purl.uniprot.org/core/author | "Morera S."xsd:string |
http://purl.uniprot.org/citations/8747457 | http://purl.uniprot.org/core/author | "Morera S."xsd:string |
http://purl.uniprot.org/citations/8747457 | http://purl.uniprot.org/core/author | "Xu Y."xsd:string |
http://purl.uniprot.org/citations/8747457 | http://purl.uniprot.org/core/author | "Xu Y."xsd:string |
http://purl.uniprot.org/citations/8747457 | http://purl.uniprot.org/core/author | "Lacombe M.-L."xsd:string |
http://purl.uniprot.org/citations/8747457 | http://purl.uniprot.org/core/author | "Lacombe M.-L."xsd:string |
http://purl.uniprot.org/citations/8747457 | http://purl.uniprot.org/core/author | "Janin J."xsd:string |
http://purl.uniprot.org/citations/8747457 | http://purl.uniprot.org/core/author | "Janin J."xsd:string |
http://purl.uniprot.org/citations/8747457 | http://purl.uniprot.org/core/author | "Lebras G."xsd:string |
http://purl.uniprot.org/citations/8747457 | http://purl.uniprot.org/core/author | "Lebras G."xsd:string |
http://purl.uniprot.org/citations/8747457 | http://purl.uniprot.org/core/date | "1995"xsd:gYear |
http://purl.uniprot.org/citations/8747457 | http://purl.uniprot.org/core/date | "1995"xsd:gYear |
http://purl.uniprot.org/citations/8747457 | http://purl.uniprot.org/core/name | "Structure"xsd:string |
http://purl.uniprot.org/citations/8747457 | http://purl.uniprot.org/core/name | "Structure"xsd:string |
http://purl.uniprot.org/citations/8747457 | http://purl.uniprot.org/core/pages | "1307-1314"xsd:string |
http://purl.uniprot.org/citations/8747457 | http://purl.uniprot.org/core/pages | "1307-1314"xsd:string |
http://purl.uniprot.org/citations/8747457 | http://purl.uniprot.org/core/title | "X-ray structure of human nucleoside diphosphate kinase B complexed with GDP at 2-A resolution."xsd:string |
http://purl.uniprot.org/citations/8747457 | http://purl.uniprot.org/core/title | "X-ray structure of human nucleoside diphosphate kinase B complexed with GDP at 2-A resolution."xsd:string |
http://purl.uniprot.org/citations/8747457 | http://purl.uniprot.org/core/volume | "3"xsd:string |
http://purl.uniprot.org/citations/8747457 | http://purl.uniprot.org/core/volume | "3"xsd:string |