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http://purl.uniprot.org/citations/11427894http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11427894http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11427894http://www.w3.org/2000/01/rdf-schema#comment"Sir2 is an NAD-dependent histone deacetylase that mediates transcriptional silencing at mating-type loci, telomeres and ribosomal gene clusters, and has a critical role in the determination of life span in yeast and Caenorhabditis elegans. The 1.7 A crystal structure of the 323 amino acid catalytic core of human SIRT2, a homolog of yeast Sir2, reveals an NAD-binding domain, which is a variant of the Rossmann fold, and a smaller domain composed of a helical module and a zinc-binding module. A conserved large groove at the interface of the two domains is the likely site of catalysis based on mutagenesis. Intersecting this large groove, there is a pocket formed by the helical module. The pocket is lined with hydrophobic residues conserved within each of the five Sir2 classes, suggesting that it is a class-specific protein-binding site."xsd:string
http://purl.uniprot.org/citations/11427894http://purl.org/dc/terms/identifier"doi:10.1038/89668"xsd:string
http://purl.uniprot.org/citations/11427894http://purl.org/dc/terms/identifier"doi:10.1038/89668"xsd:string
http://purl.uniprot.org/citations/11427894http://purl.uniprot.org/core/author"Pavletich N.P."xsd:string
http://purl.uniprot.org/citations/11427894http://purl.uniprot.org/core/author"Pavletich N.P."xsd:string
http://purl.uniprot.org/citations/11427894http://purl.uniprot.org/core/author"Donigian J.R."xsd:string
http://purl.uniprot.org/citations/11427894http://purl.uniprot.org/core/author"Donigian J.R."xsd:string
http://purl.uniprot.org/citations/11427894http://purl.uniprot.org/core/author"Finnin M.S."xsd:string
http://purl.uniprot.org/citations/11427894http://purl.uniprot.org/core/author"Finnin M.S."xsd:string
http://purl.uniprot.org/citations/11427894http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11427894http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11427894http://purl.uniprot.org/core/name"Nat. Struct. Biol."xsd:string
http://purl.uniprot.org/citations/11427894http://purl.uniprot.org/core/name"Nat. Struct. Biol."xsd:string
http://purl.uniprot.org/citations/11427894http://purl.uniprot.org/core/pages"621-625"xsd:string
http://purl.uniprot.org/citations/11427894http://purl.uniprot.org/core/pages"621-625"xsd:string
http://purl.uniprot.org/citations/11427894http://purl.uniprot.org/core/title"Structure of the histone deacetylase SIRT2."xsd:string
http://purl.uniprot.org/citations/11427894http://purl.uniprot.org/core/title"Structure of the histone deacetylase SIRT2."xsd:string
http://purl.uniprot.org/citations/11427894http://purl.uniprot.org/core/volume"8"xsd:string
http://purl.uniprot.org/citations/11427894http://purl.uniprot.org/core/volume"8"xsd:string
http://purl.uniprot.org/citations/11427894http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11427894
http://purl.uniprot.org/citations/11427894http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11427894
http://purl.uniprot.org/citations/11427894http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11427894
http://purl.uniprot.org/citations/11427894http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11427894