Thioredoxin fold
| Thioredoxin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| CDD | cd01659 | ||||||||
| Membranome | 337 | ||||||||
| |||||||||
| Thioredoxin | |
|---|---|
| Identifiers | |
| Symbol | Trx |
| Membranome | 260 |
The thioredoxin fold is a
alpha/beta protein fold that has oxidoreductase activity. The fold's spatial topology consists of a four-stranded antiparallel beta sheet sandwiched between three alpha helices
. The strand topology is 2134 with 3 antiparallel to the rest.
Sequence conservation
Despite sequence variability in many regions of the fold, thioredoxin proteins share a common
hydrophobic amino acids. The reduced form of the protein contains two free thiol
groups at the cysteine residues, whereas the oxidized form contains a disulfide bond between them.
Disulfide bond formation
Different thioredoxin fold-containing proteins vary greatly in their reactivity and in the
thiolate. Although the structure is fairly consistent among proteins containing the thioredoxin fold, the pKa is extremely sensitive to small variations in structure, especially in the placement of protein backbone
atoms near the first cysteine.
Examples
Human proteins containing this domain include:
References
- Creighton TE (2000). "Protein folding coupled to disulphide-bond formation.". In Pain RH (ed.). Mechanisms of Protein Folding (2nd ed.). Oxford University Press.