Thioredoxin

From Proteopedia

Revision as of 12:44, 13 September 2016

spinqualitylabelsall models Human thioredoxin (PDB entry 1ert) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Relevance 3 Disease 4 Structural highlights Function Thioredoxin (Trx) is an enzyme which facilitates, in its reduced form, the reduction of proteins by cysteine thiol-disulfide exchange[1]. They contain a CXXC motif. Trx-1 is a mammalian cellular protein. Trx-2 is mitochondria-specific. Trx C,M,X,Y are found in prokaryotes. Trx F,H,O are found in eukaryotes. Relevance Serum Trx level is a predictor of steatohepatitis[2]. Disease Trx is involved in a wide range of human diseases and conditions including cancer, viral diseases, aging, cardiac conditions and more[3]. Structural highlights The active site motif Cys-Gly-Pro-Cys is involved in the reduction of disulfide bonds in proteins[4]

3D Structures of Thioredoxin

Updated on 13-September-2016

References

1. ↑ Gleason FK, Holmgren A. Thioredoxin and related proteins in procaryotes. FEMS Microbiol Rev. 1988 Dec;4(4):271-97. PMID:3152490
2. ↑ Sumida Y, Nakashima T, Yoh T, Furutani M, Hirohama A, Kakisaka Y, Nakajima Y, Ishikawa H, Mitsuyoshi H, Okanoue T, Kashima K, Nakamura H, Yodoi J. Serum thioredoxin levels as a predictor of steatohepatitis in patients with nonalcoholic fatty liver disease. J Hepatol. 2003 Jan;38(1):32-8. PMID:12480557
3. ↑ Burke-Gaffney A, Callister ME, Nakamura H. Thioredoxin: friend or foe in human disease? Trends Pharmacol Sci. 2005 Aug;26(8):398-404. PMID:15990177 doi:http://dx.doi.org/10.1016/j.tips.2005.06.005
4. ↑ Weichsel A, Gasdaska JR, Powis G, Montfort WR. Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer. Structure. 1996 Jun 15;4(6):735-51. PMID:8805557