1oa8

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==Overview==
==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 ... [[http://ispc.weizmann.ac.il/pmbin/getpm?14583607 (full description)]]
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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.
==About this Structure==
==About this Structure==
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1OA8 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with NA as [[http://en.wikipedia.org/wiki/ligand ligand]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OA8 OCA]].
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1OA8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NA as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OA8 OCA].
==Reference==
==Reference==
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[[Category: rna-binding]]
[[Category: rna-binding]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:47:57 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:19:12 2007''

Revision as of 12:13, 5 November 2007


1oa8, resolution 1.70Å

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AXH DOMAIN OF HUMAN SPINOCEREBELLAR ATAXIN-1

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.

About this Structure

1OA8 is a Single protein structure of sequence from Homo sapiens with NA as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.

Reference

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

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