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http://purl.uniprot.org/citations/16677698http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16677698http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16677698http://www.w3.org/2000/01/rdf-schema#comment"Posttranslational modifications of histones regulate chromatin structure and gene expression. Histone demethylases, members of a newly emerging transcription-factor family, remove methyl groups from the lysine residues of the histone tails and thereby regulate the transcriptional activity of target genes. JmjC-domain-containing proteins have been predicted to be demethylases. For example, the JmjC-containing protein JMJD2A has been characterized as a H3-K9me3- and H3-K36me3-specific demethylase. Here, structures of the catalytic-core domain of JMJD2A with and without alpha-ketoglutarate in the presence of Fe2+ have been determined by X-ray crystallography. The structure of the core domain, consisting of the JmjN domain, the JmjC domain, the C-terminal domain, and a zinc-finger motif, revealed the unique elements that form a potential substrate binding pocket. Sited-directed mutagenesis in conjunction with demethylase activity assays allowed us to propose a molecular model for substrate selection by the JMJD2 histone demethylase family."xsd:string
http://purl.uniprot.org/citations/16677698http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2006.04.024"xsd:string
http://purl.uniprot.org/citations/16677698http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2006.04.024"xsd:string
http://purl.uniprot.org/citations/16677698http://purl.uniprot.org/core/author"Chen Z."xsd:string
http://purl.uniprot.org/citations/16677698http://purl.uniprot.org/core/author"Chen Z."xsd:string
http://purl.uniprot.org/citations/16677698http://purl.uniprot.org/core/author"Hansen K."xsd:string
http://purl.uniprot.org/citations/16677698http://purl.uniprot.org/core/author"Hansen K."xsd:string
http://purl.uniprot.org/citations/16677698http://purl.uniprot.org/core/author"Shi Y."xsd:string
http://purl.uniprot.org/citations/16677698http://purl.uniprot.org/core/author"Shi Y."xsd:string
http://purl.uniprot.org/citations/16677698http://purl.uniprot.org/core/author"Zhang G."xsd:string
http://purl.uniprot.org/citations/16677698http://purl.uniprot.org/core/author"Zhang G."xsd:string
http://purl.uniprot.org/citations/16677698http://purl.uniprot.org/core/author"Simpson M."xsd:string
http://purl.uniprot.org/citations/16677698http://purl.uniprot.org/core/author"Simpson M."xsd:string
http://purl.uniprot.org/citations/16677698http://purl.uniprot.org/core/author"Dai S."xsd:string
http://purl.uniprot.org/citations/16677698http://purl.uniprot.org/core/author"Dai S."xsd:string
http://purl.uniprot.org/citations/16677698http://purl.uniprot.org/core/author"Zang J."xsd:string
http://purl.uniprot.org/citations/16677698http://purl.uniprot.org/core/author"Zang J."xsd:string
http://purl.uniprot.org/citations/16677698http://purl.uniprot.org/core/author"Pan C.-H."xsd:string
http://purl.uniprot.org/citations/16677698http://purl.uniprot.org/core/author"Pan C.-H."xsd:string
http://purl.uniprot.org/citations/16677698http://purl.uniprot.org/core/author"Hong X."xsd:string
http://purl.uniprot.org/citations/16677698http://purl.uniprot.org/core/author"Hong X."xsd:string
http://purl.uniprot.org/citations/16677698http://purl.uniprot.org/core/author"Davrazou F."xsd:string
http://purl.uniprot.org/citations/16677698http://purl.uniprot.org/core/author"Davrazou F."xsd:string