2R2J

crystal structure of human ERp44

2R2J の概要

• エントリーDOI: 10.2210/pdb2r2j/pdb
• 分子名称: Thioredoxin domain-containing protein 4, SUCCINIC ACID, FORMIC ACID, ... (4 entities in total)
• 機能のキーワード: thioredoxin, crfs motif, chaperone, endoplasmic reticulum, stress response
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Endoplasmic reticulum lumen: Q9BS26
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 44770.87

構造登録者

Wang, L.K.,Li, S.J.,Sun, F.,Wang, C.C. (登録日: 2007-08-25, 公開日: 2008-07-08, 最終更新日: 2011-07-13)

主引用文献

Wang, L.K.,Wang, L.,Vavassori, S.,Li, S.J.,Ke, H.,Anelli, T.,Degano, M.,Ronzoni, R.,Sitia, R.,Sun, F.,Wang, C.C.
Crystal structure of human ERp44 shows a dynamic functional modulation by its carboxy-terminal tail.
Embo Rep., 2008

PubMed Abstract: ERp44 mediates thiol-dependent retention in the early secretory pathway, forming mixed disulphides with substrate proteins through its conserved CRFS motif. Here, we present its crystal structure at a resolution of 2.6 A. Three thioredoxin domains-a, b and b'-are arranged in a clover-like structure. A flexible carboxy-terminal tail turns back to the b' and a domains, shielding a hydrophobic pocket in domain b' and a hydrophobic patch around the CRFS motif in domain a. Mutational and functional studies indicate that the C-terminal tail gates the CRFS area and the adjacent hydrophobic pocket, dynamically regulating protein quality control.

PubMed: 18552768
DOI: 10.1038/embor.2008.88

実験手法

X-RAY DIFFRACTION (2.6 Å)