4AQP

The structure of the AXH domain of ataxin-1.

4AQP の概要

• エントリーDOI: 10.2210/pdb4aqp/pdb
• 関連するPDBエントリー: 1OA8 4APT
• 分子名称: ATAXIN-1, SODIUM ION, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• 機能のキーワード: rna binding protein, ob-fold, high mobility group homology, hmg
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Cytoplasm (By similarity): P54253
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 55281.77

構造登録者

Rees, M.,Chen, Y.W.,de Chiara, C.,Pastore, A. (登録日: 2012-04-19, 公開日: 2013-03-27, 最終更新日: 2023-12-20)

主引用文献

De Chiara, C.,Rees, M.,Menon, R.P.,Pauwels, K.,Lawrence, C.,Konarev, P.V.,Svergun, D.I.,Martin, S.R.,Chen, Y.W.,Pastore, A.
Self-Assembly and Conformational Heterogeneity of the Axh Domain of Ataxin-1: An Unusual Example of a Chameleon Fold
Biophys.J., 104:1304-, 2013

PubMed Abstract: Ataxin-1 is a human protein responsible for spinocerebellar ataxia type 1, a hereditary disease associated with protein aggregation and misfolding. Essential for ataxin-1 aggregation is the anomalous expansion of a polyglutamine tract near the protein N-terminus, but the sequence-wise distant AXH domain modulates and contributes to the process. The AXH domain is also involved in the nonpathologic functions of the protein, including a variety of intermolecular interactions with other cellular partners. The domain forms a globular dimer in solution and displays a dimer of dimers arrangement in the crystal asymmetric unit. Here, we have characterized the domain further by studying its behavior in the crystal and in solution. We solved two new structures of the domain crystallized under different conditions that confirm an inherent plasticity of the AXH fold. In solution, the domain is present as a complex equilibrium mixture of monomeric, dimeric, and higher molecular weight species. This behavior, together with the tendency of the AXH fold to be trapped in local conformations, and the multiplicity of protomer interfaces, makes the AXH domain an unusual example of a chameleon protein whose properties bear potential relevance for the aggregation properties of ataxin-1 and thus for disease.

PubMed: 23528090
DOI: 10.1016/J.BPJ.2013.01.048

実験手法

X-RAY DIFFRACTION (2.452 Å)