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==Overview== | ==Overview== | ||
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. | 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. | ||
==Disease== | |||
Known diseases associated with this structure: Spinocerebellar ataxia-1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=601556 601556]] | |||
==About this Structure== | ==About this Structure== | ||
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[[Category: rna-binding]] | [[Category: rna-binding]] | ||
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