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http://purl.uniprot.org/citations/16885027http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16885027http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16885027http://www.w3.org/2000/01/rdf-schema#comment"Histone methylation regulates diverse chromatin-templated processes, including transcription. Many transcriptional corepressor complexes contain lysine-specific demethylase 1 (LSD1) and CoREST that collaborate to demethylate mono- and dimethylated H3-K4 of nucleosomes. Here, we report the crystal structure of the LSD1-CoREST complex. LSD1-CoREST forms an elongated structure with a long stalk connecting the catalytic domain of LSD1 and the CoREST SANT2 domain. LSD1 recognizes a large segment of the H3 tail through a deep, negatively charged pocket at the active site and possibly a shallow groove on its surface. CoREST SANT2 interacts with DNA. Disruption of the SANT2-DNA interaction diminishes CoREST-dependent demethylation of nucleosomes by LSD1. The shape and dimension of LSD1-CoREST suggest its bivalent binding to nucleosomes, allowing efficient H3-K4 demethylation. This spatially separated, multivalent nucleosome binding mode may apply to other chromatin-modifying enzymes that generally contain multiple nucleosome binding modules."xsd:string
http://purl.uniprot.org/citations/16885027http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2006.07.012"xsd:string
http://purl.uniprot.org/citations/16885027http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2006.07.012"xsd:string
http://purl.uniprot.org/citations/16885027http://purl.uniprot.org/core/author"Luo X."xsd:string
http://purl.uniprot.org/citations/16885027http://purl.uniprot.org/core/author"Luo X."xsd:string
http://purl.uniprot.org/citations/16885027http://purl.uniprot.org/core/author"Tomchick D.R."xsd:string
http://purl.uniprot.org/citations/16885027http://purl.uniprot.org/core/author"Tomchick D.R."xsd:string
http://purl.uniprot.org/citations/16885027http://purl.uniprot.org/core/author"Yang M."xsd:string
http://purl.uniprot.org/citations/16885027http://purl.uniprot.org/core/author"Yang M."xsd:string
http://purl.uniprot.org/citations/16885027http://purl.uniprot.org/core/author"Yu H."xsd:string
http://purl.uniprot.org/citations/16885027http://purl.uniprot.org/core/author"Yu H."xsd:string
http://purl.uniprot.org/citations/16885027http://purl.uniprot.org/core/author"Borek D."xsd:string
http://purl.uniprot.org/citations/16885027http://purl.uniprot.org/core/author"Borek D."xsd:string
http://purl.uniprot.org/citations/16885027http://purl.uniprot.org/core/author"Machius M."xsd:string
http://purl.uniprot.org/citations/16885027http://purl.uniprot.org/core/author"Machius M."xsd:string
http://purl.uniprot.org/citations/16885027http://purl.uniprot.org/core/author"Otwinowski Z."xsd:string
http://purl.uniprot.org/citations/16885027http://purl.uniprot.org/core/author"Otwinowski Z."xsd:string
http://purl.uniprot.org/citations/16885027http://purl.uniprot.org/core/author"Gocke C.B."xsd:string
http://purl.uniprot.org/citations/16885027http://purl.uniprot.org/core/author"Gocke C.B."xsd:string
http://purl.uniprot.org/citations/16885027http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16885027http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16885027http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/16885027http://purl.uniprot.org/core/name"Mol. Cell"xsd:string