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http://purl.uniprot.org/citations/12897052http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12897052http://www.w3.org/2000/01/rdf-schema#comment"The chromodomain of Drosophila Polycomb protein is essential for maintaining the silencing state of homeotic genes during development. Recent studies suggest that Polycomb mediates the assembly of repressive higher-order chromatin structures in conjunction with the methylation of Lys 27 of histone H3 by a Polycomb group repressor complex. A similar mechanism in heterochromatin assembly is mediated by HP1, a chromodomain protein that binds to histone H3 methylated at Lys 9. To understand the molecular mechanism of the methyl-Lys 27 histone code recognition, we have determined a 1.4-A-resolution structure of the chromodomain of Polycomb in complex with a histone H3 peptide trimethylated at Lys 27. The structure reveals a conserved mode of methyl-lysine binding and identifies Polycomb-specific interactions with histone H3. The structure also reveals a dPC dimer in the crystal lattice that is mediated by residues specifically conserved in the Polycomb family of chromodomains. The dimerization of dPC can effectively account for the histone-binding specificity and provides new mechanistic insights into the function of Polycomb. We propose that self-association is functionally important for Polycomb."xsd:string
http://purl.uniprot.org/citations/12897052http://purl.org/dc/terms/identifier"doi:10.1101/gad.269603"xsd:string
http://purl.uniprot.org/citations/12897052http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/12897052http://purl.uniprot.org/core/author"Min J."xsd:string
http://purl.uniprot.org/citations/12897052http://purl.uniprot.org/core/author"Xu R.M."xsd:string
http://purl.uniprot.org/citations/12897052http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12897052http://purl.uniprot.org/core/name"Genes Dev"xsd:string
http://purl.uniprot.org/citations/12897052http://purl.uniprot.org/core/pages"1823-1828"xsd:string
http://purl.uniprot.org/citations/12897052http://purl.uniprot.org/core/title"Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27."xsd:string
http://purl.uniprot.org/citations/12897052http://purl.uniprot.org/core/volume"17"xsd:string
http://purl.uniprot.org/citations/12897052http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12897052
http://purl.uniprot.org/citations/12897052http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12897052
http://purl.uniprot.org/uniprot/#_P06352-mappedCitation-12897052http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12897052
http://purl.uniprot.org/uniprot/#_P26017-mappedCitation-12897052http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12897052
http://purl.uniprot.org/uniprot/#_P02299-mappedCitation-12897052http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12897052
http://purl.uniprot.org/uniprot/#_P05205-mappedCitation-12897052http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12897052
http://purl.uniprot.org/uniprot/#_Q541F9-mappedCitation-12897052http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12897052
http://purl.uniprot.org/uniprot/P02299http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/12897052
http://purl.uniprot.org/uniprot/P05205http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/12897052
http://purl.uniprot.org/uniprot/P06352http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/12897052
http://purl.uniprot.org/uniprot/P26017http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/12897052
http://purl.uniprot.org/uniprot/Q541F9http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/12897052