Thioredoxin(Trx) is a protein present in all organisms, from bacterias to complex beings as humans. This page will be focused on exploring the characteristics of Trx1, a cytosolic form of Trx present in eukaryotes. Trx1 has an active site composed of 2 cysteines separated by 2 aminoacids(Cys32 - X - X - Cys35) which catalyses the reduction of other thiol-proteins and becomes oxidized. It is reduced back by Thioredoxin Reductase(TrxR), which, in the end, is reduced by NADPH. Together, the two proteins and NADPH form the system Trx[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), a protein that produces deoxyribonucleotides from ribonucleotides[4]. Since 1964, functions of Trx1 different than participating in cell division were discovered, as denitrosation, transnitrosation, deglutathionylation,
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
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
