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http://purl.uniprot.org/citations/14583607http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14583607http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14583607http://www.w3.org/2000/01/rdf-schema#comment"Spinocerebellar ataxia type 1 is a late-onset neurodegenerative disease caused by the expansion of a CAG triplet repeat in the SCA1 gene. This results in the lengthening of a polyglutamine tract in the gene product ataxin-1. This produces a toxic gain of function that results in specific neuronal death. A region in ataxin-1, the AXH domain, exhibits significant sequence similarity to the transcription factor HBP1. This region of the protein has been implicated in RNA binding and self-association. We have determined the crystal structure of the AXH domain of ataxin-1. The AXH domain is dimeric and contains an OB-fold, a structural motif found in many oligonucleotide-binding proteins, supporting its proposed role in RNA binding. By structure comparison with other proteins that contain an OB-fold, a putative RNA-binding site has been identified. We also identified a cluster of charged surface residues that are well conserved among AXH domains. These residues may constitute a second ligand-binding surface, suggesting that all AXH domains interact with a common yet unidentified partner."xsd:string
http://purl.uniprot.org/citations/14583607http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m309817200"xsd:string
http://purl.uniprot.org/citations/14583607http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m309817200"xsd:string
http://purl.uniprot.org/citations/14583607http://purl.uniprot.org/core/author"Lowe J."xsd:string
http://purl.uniprot.org/citations/14583607http://purl.uniprot.org/core/author"Lowe J."xsd:string
http://purl.uniprot.org/citations/14583607http://purl.uniprot.org/core/author"Chen Y.W."xsd:string
http://purl.uniprot.org/citations/14583607http://purl.uniprot.org/core/author"Chen Y.W."xsd:string
http://purl.uniprot.org/citations/14583607http://purl.uniprot.org/core/author"Allen M.D."xsd:string
http://purl.uniprot.org/citations/14583607http://purl.uniprot.org/core/author"Allen M.D."xsd:string
http://purl.uniprot.org/citations/14583607http://purl.uniprot.org/core/author"Bycroft M."xsd:string
http://purl.uniprot.org/citations/14583607http://purl.uniprot.org/core/author"Bycroft M."xsd:string
http://purl.uniprot.org/citations/14583607http://purl.uniprot.org/core/author"Veprintsev D.B."xsd:string
http://purl.uniprot.org/citations/14583607http://purl.uniprot.org/core/author"Veprintsev D.B."xsd:string
http://purl.uniprot.org/citations/14583607http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14583607http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14583607http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/14583607http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/14583607http://purl.uniprot.org/core/pages"3758-3765"xsd:string
http://purl.uniprot.org/citations/14583607http://purl.uniprot.org/core/pages"3758-3765"xsd:string
http://purl.uniprot.org/citations/14583607http://purl.uniprot.org/core/title"The structure of the AXH domain of spinocerebellar ataxin-1."xsd:string
http://purl.uniprot.org/citations/14583607http://purl.uniprot.org/core/title"The structure of the AXH domain of spinocerebellar ataxin-1."xsd:string
http://purl.uniprot.org/citations/14583607http://purl.uniprot.org/core/volume"279"xsd:string
http://purl.uniprot.org/citations/14583607http://purl.uniprot.org/core/volume"279"xsd:string