4WTH

Ataxin-3 Carboxy Terminal Region - Crystal C2 (triclinic)

4WTH の概要

• エントリーDOI: 10.2210/pdb4wth/pdb
• 関連するPDBエントリー: 4YS9
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: Maltose-binding periplasmic protein, Ataxin-3 chimera, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ZINC ION, ... (4 entities in total)
• 機能のキーワード: ataxin-3, polyglutamine helix, nerve tissue proteins, polyq, triplet repeat disorder, transcription
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 98229.92

構造登録者

Zhemkov, V.A.,Kim, M. (登録日: 2014-10-30, 公開日: 2016-03-09, 最終更新日: 2023-09-27)

主引用文献

Zhemkov, V.A.,Kulminskaya, A.A.,Bezprozvanny, I.B.,Kim, M.
The 2.2-Angstrom resolution crystal structure of the carboxy-terminal region of ataxin-3.
FEBS Open Bio, 6:168-178, 2016

PubMed Abstract: An expansion of polyglutamine (polyQ) sequence in ataxin-3 protein causes spinocerebellar ataxia type 3, an inherited neurodegenerative disorder. The crystal structure of the polyQ-containing carboxy-terminal fragment of human ataxin-3 was solved at 2.2-Å resolution. The Atxn3 carboxy-terminal fragment including 14 glutamine residues adopts both random coil and α-helical conformations in the crystal structure. The polyQ sequence in α-helical structure is stabilized by intrahelical hydrogen bonds mediated by glutamine side chains. The intrahelical hydrogen-bond interactions between glutamine side chains along the axis of the polyQ α-helix stabilize the secondary structure. Analysis of this structure furthers our understanding of the polyQ-structural characteristics that likely underlie the pathogenesis of polyQ-expansion disorders.

PubMed: 27047745
DOI: 10.1002/2211-5463.12029

実験手法

X-RAY DIFFRACTION (2.25 Å)