User:Arthur Migliatti/Sandbox1

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You may include any references to papers as in: the use of JSmol in Proteopedia ^[1] or to the article describing Jmol ^[2] to the rescue.

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, mithocondrial and secreted. Fazer distinção antes sobre a Trx1 e a Trx2. Não sei se a Trx2 também possui sítio ativo nesse lugar.

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

Falar da RNR, Prx e outras proteínas que eu tenho visto que ela interage.

Disease

Relevance

Structural highlights

Post-translational changes

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