1oa8: Difference between revisions
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'''AXH DOMAIN OF HUMAN SPINOCEREBELLAR ATAXIN-1''' | '''AXH DOMAIN OF HUMAN SPINOCEREBELLAR ATAXIN-1''' | ||
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[[Category: Bycroft, M.]] | [[Category: Bycroft, M.]] | ||
[[Category: Chen, Y W.]] | [[Category: Chen, Y W.]] | ||
[[Category: | [[Category: High mobility group homology]] | ||
[[Category: | [[Category: Hmg]] | ||
[[Category: | [[Category: Rna-binding,dimerization]] | ||
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Revision as of 03:35, 3 May 2008
AXH DOMAIN OF HUMAN SPINOCEREBELLAR ATAXIN-1
OverviewOverview
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.
About this StructureAbout this Structure
1OA8 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
The structure of the AXH domain of spinocerebellar ataxin-1., Chen YW, Allen MD, Veprintsev DB, Lowe J, Bycroft M, J Biol Chem. 2004 Jan 30;279(5):3758-65. Epub 2003 Oct 28. PMID:14583607 Page seeded by OCA on Sat May 3 03:35:18 2008