5W1L

Echinococcus granulosus thioredoxin glutathione reductas (egTGR) with Gold

5W1L の概要

• エントリーDOI: 10.2210/pdb5w1l/pdb
• 関連するPDBエントリー: 5W1J
• 分子名称: Thioredoxin glutathione reductase, FLAVIN-ADENINE DINUCLEOTIDE, GOLD ION, ... (4 entities in total)
• 機能のキーワード: egtgr, redox, antioxidant, signaling protein
• 由来する生物種: Echinococcus granulosus (Hydatid tapeworm); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 130871.98

構造登録者

Gao, W.,Wang, Y.,Dai, S. (登録日: 2017-06-03, 公開日: 2017-11-22, 最終更新日: 2024-10-23)

主引用文献

Salinas, G.,Gao, W.,Wang, Y.,Bonilla, M.,Yu, L.,Novikov, A.,Virginio, V.G.,Ferreira, H.B.,Vieites, M.,Gladyshev, V.N.,Gambino, D.,Dai, S.
The Enzymatic and Structural Basis for Inhibition of Echinococcus granulosus Thioredoxin Glutathione Reductase by Gold(I).
Antioxid. Redox Signal., 27:1491-1504, 2017

PubMed Abstract: New drugs are needed to treat flatworm infections that cause severe human diseases such as schistosomiasis. The unique flatworm enzyme thioredoxin glutathione reductase (TGR), structurally different from the human enzyme, is a key drug target. Structural studies of the flatworm Echinococcus granulosus TGR, free and complexed with Au-MPO, a novel gold inhibitor, together with inhibition assays were performed.

PubMed: 28463568
DOI: 10.1089/ars.2016.6816

実験手法

X-RAY DIFFRACTION (2.88 Å)