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Thioredoxin(Trx) is a protein present in all organisms, from bacterias to complex beings as humans. It has an active site composed of 2 cysteines separated by 2 aminoacids(Cys32 - X - X - Cys35). Trx interacts with a diverse pool of proteins, acting, when reduced, as a donator of a pair of electrons, and becomes oxidized, being reduced back by Thioredoxin Reductase(TrxR), which is reduced in the end by NADPH [3]. Trx and TrxR were first discovered in 1964 in a study realized in bacteria, and were described as necessary proteins to reduce Ribonucleotide Reductase(RNR), an enzyme involved in DNA replication and repair.
Cytosolic, nuclear and secreted.
Structure
One 4 strands beta sheet involved by 5 alpha-helix. Primary structure depends on the organism. Yeast Trx (yTrx) has only 2 cysteines, the ones in the active site. Human Trx, on the other hand has 5 cysteines: Cys32, Cys35, which composes the active site, Cys62, Cys 69, structural cysteines, and Cys73, an important sensor against oxidative conditions.
Function
Disease
Relevance
Structural highlights
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