5W1L

Echinococcus granulosus thioredoxin glutathione reductas (egTGR) with Gold

Summary for 5W1L

• Entry DOI: 10.2210/pdb5w1l/pdb
• Related: 5W1J
• Descriptor: Thioredoxin glutathione reductase, FLAVIN-ADENINE DINUCLEOTIDE, GOLD ION, ... (4 entities in total)
• Functional Keywords: egtgr, redox, antioxidant, signaling protein
• Biological source: Echinococcus granulosus (Hydatid tapeworm); More
• Total number of polymer chains: 2
• Total formula weight: 130871.98

Authors

Gao, W.,Wang, Y.,Dai, S. (deposition date: 2017-06-03, release date: 2017-11-22, Last modification date: 2024-10-23)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.88 Å)