4JU5

Crystal structure of the dimeric form of the bb' domains of human protein disulfide isomerase

4JU5 の概要

• エントリーDOI: 10.2210/pdb4ju5/pdb
• 分子名称: Protein disulfide-isomerase (2 entities in total)
• 機能のキーワード: thioredoxin-like fold, disulfide isomerase, chaperone, isomerase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 53670.51

構造登録者

Bastos-Aristizabal, S.,Kozlov, G.,Gehring, K. (登録日: 2013-03-24, 公開日: 2014-02-19, 最終更新日: 2023-09-20)

主引用文献

Bastos-Aristizabal, S.,Kozlov, G.,Gehring, K.
Structural insight into the dimerization of human protein disulfide isomerase.
Protein Sci., 23:618-626, 2014

PubMed Abstract: Protein disulfide isomerases (PDIs) are responsible for catalyzing the proper oxidation and isomerization of disulfide bonds of newly synthesized proteins in the endoplasmic reticulum (ER). Here, it is shown that human PDI (PDIA1) dimerizes in vivo and proposed that the dimerization of PDI has physiological relevance by autoregulating its activity. The crystal structure of the dimeric form of noncatalytic bb' domains of human PDIA1 determined to 2.3 Å resolution revealed that the formation of dimers occludes the substrate binding site and may function as a mechanism to regulate PDI activity in the ER.

PubMed: 24549644
DOI: 10.1002/pro.2444

実験手法

X-RAY DIFFRACTION (2.28 Å)