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Thioredoxin
From Proteopedia
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| - | + | <StructureSection load='' size='350' side='right' caption='Human thioredoxin (PDB entry [[1ert]])' scene='43/430885/Cv/2'> | |
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| - | [[Thioredoxin]] (Trx) is an enzyme which facilitates the reduction of proteins by cysteine thiol-disulfide exchange. They contain a CXXC motif. Trx-1 is a mammalian cellular protein. Trx-2 is mitochondria-specific. | + | == Function == |
| + | [[Thioredoxin]] (Trx) is an enzyme which facilitates, in its reduced form, the reduction of proteins by cysteine thiol-disulfide exchange<ref>PMID:3152490</ref>. They contain a CXXC motif.<br /> | ||
| + | * '''Trx-1''' is a mammalian cellular protein.<br /> | ||
| + | * '''Trx-2''' is mitochondria-specific.<br /> | ||
| + | * '''Trx C,M,X,Y''' are found in prokaryotes.<br /> | ||
| + | * '''Trx F,H,O''' are found in eukaryotes.<br /> | ||
| - | {{TOC limit|limit=2}} | ||
| - | == | + | == Relevance == |
| + | Serum Trx level is a predictor of steatohepatitis<ref>PMID:12480557</ref>. | ||
| + | == Disease == | ||
| + | Trx is involved in a wide range of human diseases and conditions including cancer, viral diseases, aging, cardiac conditions and more<ref>PMID:15990177</ref>. | ||
| + | == Structural highlights == | ||
| + | The <scene name='43/430885/Cv/4'>active site motif Cys-Gly-Pro-Cys</scene> is involved in the reduction of disulfide bonds in proteins<ref>PMID:8805557</ref> | ||
| - | == | + | == 3D Structures of Thioredoxin == |
| - | + | [[Thioredoxin 3D structures]] | |
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| - | + | </StructureSection> | |
| - | + | == References == | |
| - | + | <references/> | |
| + | [[Category:Topic Page]] | ||
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References
- ↑ Gleason FK, Holmgren A. Thioredoxin and related proteins in procaryotes. FEMS Microbiol Rev. 1988 Dec;4(4):271-97. PMID:3152490
- ↑ 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
- ↑ 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
- ↑ 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

