5V90

Crystal structure of ERp29 D-domain in complex with the P-domain of calreticulin

5V90 の概要

• エントリーDOI: 10.2210/pdb5v90/pdb
• 関連するPDBエントリー: 5V8Z
• 分子名称: Endoplasmic reticulum resident protein 29, Calreticulin, GLYCEROL (3 entities in total)
• 機能のキーワード: chaperone, protein binding, protein folding
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 33229.43

構造登録者

Kozlov, G.,Munoz-Escobar, J.,Gehring, K. (登録日: 2017-03-22, 公開日: 2017-06-21, 最終更新日: 2023-10-04)

主引用文献

Kozlov, G.,Munoz-Escobar, J.,Castro, K.,Gehring, K.
Mapping the ER Interactome: The P Domains of Calnexin and Calreticulin as Plurivalent Adapters for Foldases and Chaperones.
Structure, 25:1415-1422.e3, 2017

PubMed Abstract: The lectin chaperones calreticulin (CRT) and calnexin (CNX) contribute to the folding of glycoproteins in the ER by recruiting foldases such as the protein disulfide isomerase ERp57 and the peptidyl prolyl cis-trans isomerase CypB. Recently, CRT was shown to interact with the chaperone ERp29. Here, we show that ERp29 directly binds to the P domain of CNX. Crystal structures of the D domain of ERp29 in complex with the P domains from CRT and calmegin, a tissue-specific CNX homolog, reveal a commonality in the mechanism of binding whereby the tip of the P domain functions as a plurivalent adapter to bind a variety of folding factors. We show that mutation of a single residue, D348 in CNX, abrogates binding to ERp29 as well as ERp57 and CypB. The structural diversity of the accessory factors suggests that these chaperones became specialized for glycoprotein folding through convergent evolution of their P-domain binding sites.

PubMed: 28877505
DOI: 10.1016/j.str.2017.07.010

実験手法

X-RAY DIFFRACTION (3.255 Å)