1G7D

NMR STRUCTURE OF ERP29 C-DOMAIN

1G7D の概要

• エントリーDOI: 10.2210/pdb1g7d/pdb
• 関連するPDBエントリー: 1G7E
• 分子名称: ENDOPLASMIC RETICULUM PROTEIN ERP29 (1 entity in total)
• 機能のキーワード: alpha helical protein, chaperone
• 由来する生物種: Rattus norvegicus (Norway rat)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11787.47

構造登録者

Liepinsh, E.,Mkrtchian, S.,Barishev, M.,Sharipo, A.,Ingelman-Sundberg, M.,Otting, G. (登録日: 2000-11-10, 公開日: 2000-11-29, 最終更新日: 2024-05-22)

主引用文献

Liepinsh, E.,Baryshev, M.,Sharipo, A.,Ingelman-Sundberg, M.,Otting, G.,Mkrtchian, S.
Thioredoxin fold as homodimerization module in the putative chaperone ERp29: NMR structures of the domains and experimental model of the 51 kDa dimer.
Structure, 9:457-471, 2001

PubMed Abstract: ERp29 is a ubiquitously expressed rat endoplasmic reticulum (ER) protein conserved in mammalian species. Fold predictions suggest the presence of a thioredoxin-like domain homologous to the a domain of human protein disulfide isomerase (PDI) and a helical domain similar to the C-terminal domain of P5-like PDIs. As ERp29 lacks the double-cysteine motif essential for PDI redox activity, it is suggested to play a role in protein maturation and/or secretion related to the chaperone function of PDI. ERp29 self-associates into 51 kDa dimers and also higher oligomers.

PubMed: 11435111
DOI: 10.1016/S0969-2126(01)00607-4

実験手法

SOLUTION NMR