Thioredoxin-like%20superfamily QuickView

Description:: Several biological processes regulate the activity of target proteins through changes in the redox state of thiol groups (S2 to SH2), where a hydrogen donor is linked to an intermediary disulphide protein. Such processes include the ferredoxin/thioredoxin system, the NADP/thioredoxin system, and the glutathione/glutaredoxin system. Several of these disulphide proteins share a common structure, consisting of a three-layer alpha/beta/alpha core. Proteins that contain domains with a thioredoxin-like fold include:Arsenate reductase (ArsC)Calsequestrin (contains three tandem repeats of this fold)Circadian oscillation regulator KaiBDisulphide bond isomerase DsbC and DsbG (C-terminal domain)Disulphide bond facilitator DsbA (contains an alpha-helical insertion)Endoplasmic reticulum protein ERP29 (N-terminal domain)Glutathione S-transferase (GST) (N-terminal domain)Mitochondrial ribosomal protein L51/S25/CI-B8 domain (variable positions for Cys residues in active site)PhosducinProtein disulphide isomerase (PDI) (contains two tandem repeats of this fold)Glutathione peroxidase-like enzymesSelenoprotein W-relatedSH3-binding glutamic acid-rich protein like (SH3BGR) (lacks both conserved Cys residues)Spliceosomal protein U5-15KdThioltransferases, including thioredoxin, glutaredoxon, hybrid peroxiredoxin hyPrx5Thioredoxin-like 2Fe-2S ferredoxin