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http://purl.uniprot.org/citations/11226167http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11226167http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11226167http://www.w3.org/2000/01/rdf-schema#comment"Plant homeodomain (PHD) domains are found in >400 eukaryotic proteins, many of which are transcriptional regulators. Naturally occurring point mutations or deletions of this domain contribute to a variety of human diseases, including ATRX syndrome, myeloid leukemias and autoimmune dysfunction. Here we report the first structural characterization of a PHD domain. Our studies reveal that the PHD domain from KAP-1 corepressor binds zinc in a cross-brace topology between anti-parallel ss-strands reminiscent of RING (really interesting new gene) domains. Using a mutational analysis, we define the structural features required for transcriptional repression by KAP-1 and explain naturally occurring, disease-causing mutations in PHD domains of other proteins. From a comparison of this PHD structure with previously reported RING and LIM (Lin11/Isl-1/Mec-3) structures, we infer sequence determinants that allow discrimination among PHD, RING and LIM motifs."xsd:string
http://purl.uniprot.org/citations/11226167http://purl.org/dc/terms/identifier"doi:10.1093/emboj/20.1.165"xsd:string
http://purl.uniprot.org/citations/11226167http://purl.org/dc/terms/identifier"doi:10.1093/emboj/20.1.165"xsd:string
http://purl.uniprot.org/citations/11226167http://purl.uniprot.org/core/author"Rauscher F.J. III"xsd:string
http://purl.uniprot.org/citations/11226167http://purl.uniprot.org/core/author"Rauscher F.J. III"xsd:string
http://purl.uniprot.org/citations/11226167http://purl.uniprot.org/core/author"Schultz D.C."xsd:string
http://purl.uniprot.org/citations/11226167http://purl.uniprot.org/core/author"Schultz D.C."xsd:string
http://purl.uniprot.org/citations/11226167http://purl.uniprot.org/core/author"Borden K.L."xsd:string
http://purl.uniprot.org/citations/11226167http://purl.uniprot.org/core/author"Borden K.L."xsd:string
http://purl.uniprot.org/citations/11226167http://purl.uniprot.org/core/author"Capili A.D."xsd:string
http://purl.uniprot.org/citations/11226167http://purl.uniprot.org/core/author"Capili A.D."xsd:string
http://purl.uniprot.org/citations/11226167http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11226167http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11226167http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/11226167http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/11226167http://purl.uniprot.org/core/pages"165-177"xsd:string
http://purl.uniprot.org/citations/11226167http://purl.uniprot.org/core/pages"165-177"xsd:string
http://purl.uniprot.org/citations/11226167http://purl.uniprot.org/core/title"Solution structure of the PHD domain from the KAP-1 corepressor: structural determinants for PHD, RING and LIM zinc-binding domains."xsd:string
http://purl.uniprot.org/citations/11226167http://purl.uniprot.org/core/title"Solution structure of the PHD domain from the KAP-1 corepressor: structural determinants for PHD, RING and LIM zinc-binding domains."xsd:string
http://purl.uniprot.org/citations/11226167http://purl.uniprot.org/core/volume"20"xsd:string
http://purl.uniprot.org/citations/11226167http://purl.uniprot.org/core/volume"20"xsd:string
http://purl.uniprot.org/citations/11226167http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11226167
http://purl.uniprot.org/citations/11226167http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11226167