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http://purl.uniprot.org/citations/17412961http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17412961http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17412961http://www.w3.org/2000/01/rdf-schema#comment"Although highly homologous, the spliceosomal hPrp31 and the nucleolar Nop56 and Nop58 (Nop56/58) proteins recognize different ribonucleoprotein (RNP) particles. hPrp31 interacts with complexes containing the 15.5K protein and U4 or U4atac small nuclear RNA (snRNA), whereas Nop56/58 associate with 15.5K-box C/D small nucleolar RNA complexes. We present structural and biochemical analyses of hPrp31-15.5K-U4 snRNA complexes that show how the conserved Nop domain in hPrp31 maintains high RNP binding selectivity despite relaxed RNA sequence requirements. The Nop domain is a genuine RNP binding module, exhibiting RNA and protein binding surfaces. Yeast two-hybrid analyses suggest a link between retinitis pigmentosa and an aberrant hPrp31-hPrp6 interaction that blocks U4/U6-U5 tri-snRNP formation."xsd:string
http://purl.uniprot.org/citations/17412961http://purl.org/dc/terms/identifier"doi:10.1126/science.1137924"xsd:string
http://purl.uniprot.org/citations/17412961http://purl.org/dc/terms/identifier"doi:10.1126/science.1137924"xsd:string
http://purl.uniprot.org/citations/17412961http://purl.uniprot.org/core/author"Li P."xsd:string
http://purl.uniprot.org/citations/17412961http://purl.uniprot.org/core/author"Li P."xsd:string
http://purl.uniprot.org/citations/17412961http://purl.uniprot.org/core/author"Liu S."xsd:string
http://purl.uniprot.org/citations/17412961http://purl.uniprot.org/core/author"Liu S."xsd:string
http://purl.uniprot.org/citations/17412961http://purl.uniprot.org/core/author"Wahl M.C."xsd:string
http://purl.uniprot.org/citations/17412961http://purl.uniprot.org/core/author"Wahl M.C."xsd:string
http://purl.uniprot.org/citations/17412961http://purl.uniprot.org/core/author"Carlomagno T."xsd:string
http://purl.uniprot.org/citations/17412961http://purl.uniprot.org/core/author"Carlomagno T."xsd:string
http://purl.uniprot.org/citations/17412961http://purl.uniprot.org/core/author"Luehrmann R."xsd:string
http://purl.uniprot.org/citations/17412961http://purl.uniprot.org/core/author"Luehrmann R."xsd:string
http://purl.uniprot.org/citations/17412961http://purl.uniprot.org/core/author"Dybkov O."xsd:string
http://purl.uniprot.org/citations/17412961http://purl.uniprot.org/core/author"Dybkov O."xsd:string
http://purl.uniprot.org/citations/17412961http://purl.uniprot.org/core/author"Hartmuth K."xsd:string
http://purl.uniprot.org/citations/17412961http://purl.uniprot.org/core/author"Hartmuth K."xsd:string
http://purl.uniprot.org/citations/17412961http://purl.uniprot.org/core/author"Nottrott S."xsd:string
http://purl.uniprot.org/citations/17412961http://purl.uniprot.org/core/author"Nottrott S."xsd:string
http://purl.uniprot.org/citations/17412961http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17412961http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17412961http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/17412961http://purl.uniprot.org/core/name"Science"xsd:string