4I6X

Crystal Structure of Non-catalyic Domain of Protein Disulfide Isomerase-related (PDIr) Protein

4I6X の概要

• エントリーDOI: 10.2210/pdb4i6x/pdb
• 分子名称: Protein disulfide-isomerase A5 (2 entities in total)
• 機能のキーワード: thioredoxin-like fold, protein binding, endoplasmic reticulum, isomerase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Endoplasmic reticulum lumen (By similarity): Q14554
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15024.34

構造登録者

Kozlov, G.,Vinaik, R.,Gehring, K. (登録日: 2012-11-30, 公開日: 2013-04-03, 最終更新日: 2024-11-06)

主引用文献

Vinaik, R.,Kozlov, G.,Gehring, K.
Structure of the Non-Catalytic Domain of the Protein Disulfide Isomerase-Related Protein (PDIR) Reveals Function in Protein Binding.
Plos One, 8:e62021-e62021, 2013

PubMed Abstract: Protein disulfide isomerases comprise a large family of enzymes responsible for catalyzing the proper oxidation and folding of newly synthesized proteins in the endoplasmic reticulum (ER). Protein disulfide isomerase-related (PDIR) protein (also known as PDIA5) is a specialized member that participates in the folding of α1-antitrypsin and N-linked glycoproteins. Here, the crystal structure of the non-catalytic domain of PDIR was determined to 1.5 Å resolution. The structure adopts a thioredoxin-like fold stabilized by a structural disulfide bridge with a positively charged binding surface for interactions with the ER chaperones, calreticulin and ERp72. Crystal contacts between molecules potentially mimic the interactions of PDIR with misfolded substrate proteins. The results suggest that the non-catalytic domain of PDIR plays a key role in the recognition of protein partners and substrates.

PubMed: 23614004
DOI: 10.1371/journal.pone.0062021

実験手法

X-RAY DIFFRACTION (1.5 Å)