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 is involved in the reduction of disulfide bonds in proteins[4]

3D Structures of Thioredoxin

Thioredoxin 3D structures


Human thioredoxin (PDB entry 1ert)

Drag the structure with the mouse to rotate

ReferencesReferences

  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

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