1OA8

AXH domain of human spinocerebellar ataxin-1

Summary for 1OA8

• Entry DOI: 10.2210/pdb1oa8/pdb
• Descriptor: ATAXIN-1, SODIUM ION (3 entities in total)
• Functional Keywords: rna binding, high mobility group homology, hmg, rna-binding, dimerization
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 4
• Total formula weight: 57782.33

Authors

Allen, M.D.,Chen, Y.W.,Bycroft, M. (deposition date: 2003-01-02, release date: 2003-11-06, Last modification date: 2024-05-08)

Primary citation

Chen, Y.W.,Allen, M.D.,Veprintsev, D.B.,Lowe, J.,Bycroft, M.
The structure of the AXH domain of spinocerebellar ataxin-1.
J. Biol. Chem., 279:3758-3765, 2004

PubMed Abstract: 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.

PubMed: 14583607
DOI: 10.1074/jbc.M309817200

Experimental method

X-RAY DIFFRACTION (1.7 Å)