Thioredoxin Glutathione Reductase
From Proteopedia
Image:2v6o.png
Crystal Structure of Thioredoxin Glutathione Reductase (2v6o)
Contents |
Function
Thioredoxin Glutathione Reductase (TGR) is an enzyme which bridges two detoxification pathways[1]. It is composed of a small glutaredoxin domain at the N-terminal and a large thioredoxin reductase one at the C-terminal.
Relevance
TGR is a therpeutic drug target against schistosomiasis[2].
3D Structures of Thioredoxin Glutathione Reductase
2v6o, 2x8c, 2x8g, 2x8h – SmTGR+FAD – Schistosoma mansoni
2x99 - SmTGR+FAD+NADPH
3h4k - SmTGR+FAD+auranofin
4la1 - TGR+FAD – Schistosoma japonicum
References
- ↑ Prast-Nielsen S, Huang HH, Williams DL. Thioredoxin glutathione reductase: its role in redox biology and potential as a target for drugs against neglected diseases. Biochim Biophys Acta. 2011 Dec;1810(12):1262-71. doi:, 10.1016/j.bbagen.2011.06.024. Epub 2011 Jul 14. PMID:21782895 doi:http://dx.doi.org/10.1016/j.bbagen.2011.06.024
- ↑ Song L, Li J, Xie S, Qian C, Wang J, Zhang W, Yin X, Hua Z, Yu C. Thioredoxin glutathione reductase as a novel drug target: evidence from Schistosoma japonicum. PLoS One. 2012;7(2):e31456. doi: 10.1371/journal.pone.0031456. Epub 2012 Feb 22. PMID:22384025 doi:http://dx.doi.org/10.1371/journal.pone.0031456
