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http://purl.uniprot.org/citations/15933070http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15933070http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15933070http://www.w3.org/2000/01/rdf-schema#comment"SET8 (also known as PR-SET7) is a histone H4-Lys-20-specific methyltransferase that is implicated in cell-cycle-dependent transcriptional silencing and mitotic regulation in metazoans. Herein we report the crystal structure of human SET8 (hSET8) bound to a histone H4 peptide bearing Lys-20 and the product cofactor S-adenosylhomocysteine. Histone H4 intercalates in the substrate-binding cleft as an extended parallel beta-strand. Residues preceding Lys-20 in H4 engage in an extensive array of salt bridge, hydrogen bond, and van der Waals interactions with hSET8, while the C-terminal residues bind through predominantly hydrophobic interactions. Mutational analysis of both the substrate-binding cleft and histone H4 reveals that interactions with residues in the N and C termini of the H4 peptide are critical for conferring substrate specificity. Finally, analysis of the product specificity indicates that hSET8 is a monomethylase, consistent with its role in the maintenance of Lys-20 monomethylation during cell division."xsd:string
http://purl.uniprot.org/citations/15933070http://purl.org/dc/terms/identifier"doi:10.1101/gad.1318405"xsd:string
http://purl.uniprot.org/citations/15933070http://purl.org/dc/terms/identifier"doi:10.1101/gad.1318405"xsd:string
http://purl.uniprot.org/citations/15933070http://purl.uniprot.org/core/author"Brunzelle J.S."xsd:string
http://purl.uniprot.org/citations/15933070http://purl.uniprot.org/core/author"Brunzelle J.S."xsd:string
http://purl.uniprot.org/citations/15933070http://purl.uniprot.org/core/author"Trievel R.C."xsd:string
http://purl.uniprot.org/citations/15933070http://purl.uniprot.org/core/author"Trievel R.C."xsd:string
http://purl.uniprot.org/citations/15933070http://purl.uniprot.org/core/author"Couture J.-F."xsd:string
http://purl.uniprot.org/citations/15933070http://purl.uniprot.org/core/author"Couture J.-F."xsd:string
http://purl.uniprot.org/citations/15933070http://purl.uniprot.org/core/author"Collazo E."xsd:string
http://purl.uniprot.org/citations/15933070http://purl.uniprot.org/core/author"Collazo E."xsd:string
http://purl.uniprot.org/citations/15933070http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15933070http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15933070http://purl.uniprot.org/core/name"Genes Dev."xsd:string
http://purl.uniprot.org/citations/15933070http://purl.uniprot.org/core/name"Genes Dev."xsd:string
http://purl.uniprot.org/citations/15933070http://purl.uniprot.org/core/pages"1455-1465"xsd:string
http://purl.uniprot.org/citations/15933070http://purl.uniprot.org/core/pages"1455-1465"xsd:string
http://purl.uniprot.org/citations/15933070http://purl.uniprot.org/core/title"Structural and functional analysis of SET8, a histone H4 'Lys-20' methyltransferase."xsd:string
http://purl.uniprot.org/citations/15933070http://purl.uniprot.org/core/title"Structural and functional analysis of SET8, a histone H4 'Lys-20' methyltransferase."xsd:string
http://purl.uniprot.org/citations/15933070http://purl.uniprot.org/core/volume"19"xsd:string
http://purl.uniprot.org/citations/15933070http://purl.uniprot.org/core/volume"19"xsd:string
http://purl.uniprot.org/citations/15933070http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15933070
http://purl.uniprot.org/citations/15933070http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15933070