AXHdomain in Ataxins and HMG containing proteins |
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| SMART accession number: | SM00536
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| Description: |
unknown function |
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| Interpro abstract (IPR003652): |
Spinocerebellar ataxia type 1 is late-onset neurodegenerative diseases 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 producing a toxic gain of function that results in neuronal death. The crystal structure of the AXH domain of ataxin-1 has been determined as it exhibits significant sequence similarity to the transcription factor HBP1 [(PUBMED:12965213)] and has been implicated in RNA binding and self-association. The AXH domain is dimeric and contains an OB-fold, a structural motif found in many oligonucleotide-binding proteins. By comparison to other proteins that contain an OB-fold, the putative RNA-binding region has been identified. In addition, there are a number of well-conserved residues that form a second ligand-binding surface, suggesting that AXH domains interact with a common yet unidentified partner [(PUBMED:14583607)].
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| GO function: | protein binding (GO:0005515), RNA binding (GO:0003723) |
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| Family alignment: |
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There are 27
AXH domains in 27 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
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- Literature (relevant references for this domain)
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Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Burright EN, Davidson JD, Duvick LA, Koshy B, Zoghbi HY, Orr HT
- Identification of a self-association region within the SCA1 gene product, ataxin-1.
- Hum Mol Genet. 1997; 6: 513-8
- Display abstract
Spinocerebellar ataxia type 1 (SCA1) is an autosomal dominant neurodegenerative disorder caused by the expansion of a polyglutamine tract within the SCA1 gene product, ataxin-1. Expansion of this tract is believed to result in a gain of function by the mutant protein, perhaps through altered self-associations or interactions with other cellular proteins. We have used the yeast two hybrid system to determine if ataxin-1 is capable of multimerization. This analysis revealed that ataxin-1 does have the ability to self-associate, however, this association does not appear to be influenced by expansion of the polyglutamine tract. Consistent with this finding, deletion analysis excluded the involvement of the polyglutamine tract in ataxin-1 self-association, and instead localized the multimerization region to amino acids 495-605 of the wild type protein. These results, while identifying an ataxin-1 self-interaction region, fail to support a proposed model of polar-zipper mediated multimerization involving the ataxin-1 polyglutamine tract.
- Quan F, Janas J, Popovich BW
- A novel CAG repeat configuration in the SCA1 gene: implications for the molecular diagnostics of spinocerebellar ataxia type 1.
- Hum Mol Genet. 1995; 4: 2411-3
- Structure (3D structures containing this domain)
3D Structures of AXH domains in PDB
| PDB code | Main view | Title | | 1oa8 |  | Axh domain of human spinocerebellar ataxin-1 |
| 1v06 |  | Axh domain of the transcription factor hbp1 from m.musculus |
- Links (links to other resources describing this domain)
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to expand nodes. To display all proteins with a AXH domain in a specific node, click on it.