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| {{STRUCTURE_1oa8| PDB=1oa8 | SCENE= }} | | {{STRUCTURE_1oa8| PDB=1oa8 | SCENE= }} |
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| '''AXH DOMAIN OF HUMAN SPINOCEREBELLAR ATAXIN-1'''
| | ===AXH DOMAIN OF HUMAN SPINOCEREBELLAR ATAXIN-1=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_14583607}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 14583607 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_14583607}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Hmg]] | | [[Category: Hmg]] |
| [[Category: Rna-binding,dimerization]] | | [[Category: Rna-binding,dimerization]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:35:18 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:07:46 2008'' |
