| Abstract | 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 [ 15862094]. Several of these disulphide proteins share a common structure, consisting of a three-layer alpha/beta/alpha core. Proteins that contain this thioredoxin fold include: 2Fe-2S ferredoxin, thioltransferase, phosducin, glutathione peroxidase-like enzymes, arsenate reductase, disulphide bond isomerase DsbC (C-terminal domain), disulphide bond facilitator DsbA (contains an alpha-helical insertion), glutathione S-transferase (N-terminal domain), Endoplasmic reticulum protein ERP29 (N-terminal domain), spliceosomal protein U5-15Kd, circadian oscillation regulator KaiB, protein disulphide isomerase PDI (contains two tandem repeats of this fold), and calsequestrin (contains three tandem repeats of this fold).
This entry differs from the thioredoxin fold protein, the classification of this fold is in the glutathione S-transferase enzymes, where this entry defines two regions containing this fold, and the thioredoxin fold protein defines only the N-terminal as containing this fold.
|
0
