Thioredoxin
Human thioredoxin | ||
---|---|---|
Ribbon model (right), surface model (left) of the thioredoxin dimer (reduced form) according to PDB 1AIU . Catalytic amino acids 35–37 shown as domes. | ||
Properties of human protein | ||
Mass / length primary structure | 104 amino acids | |
Secondary to quaternary structure | Homodimer | |
Identifier | ||
Gene names | TXN ; TRDX; TRX | |
External IDs | ||
Occurrence | ||
Homology family | Thioredoxin | |
Parent taxon | Creature | |
Orthologue | ||
human | House mouse | |
Entrez | 7295 | 22166 |
Ensemble | ENSG00000136810 | ENSMUSG00000028367 |
UniProt | P10599 | P10639 |
Refseq (mRNA) | NM_001244938 | NM_011660 |
Refseq (protein) | NP_001231867 | NP_035790 |
Gene locus | Chr 9: 110.24 - 110.26 Mb | Chr 4: 57.94 - 57.96 Mb |
PubMed search | 7295 |
22166
|
Thioredoxins are small proteins with around 100 amino acids and a disulfide bridge as an active center, which are of great importance as electron-transferring cofactors in practically all organisms. In the reduced form, thioredoxins act enzymatically as oxidoreductase . Two thioredoxins are known in humans, depending on their location in the cytoplasm or the mitochondria . From studies in rats there is evidence of a role as an antioxidant and regulator of biomechanical signal transduction . Thioredoxin is not to be confused with the family of proteins that contain a thioredoxin domain . Thioredoxin binds to TXNIP .
In plants, thioredoxins play a key role in the regulation of the primary carbon change: They control the activity of enzymes of the Calvin cycle , the Rubisco activase, and support the assembly of the CF1 subunit of the ATP synthase .
structure
Thioredoxins weigh about 12 kDa . In their active center, which is directed outwards, they carry the sequence cysteine - glycine - proline - cysteine , which is responsible for the electron transfers . The two cysteine groups can assume two different redox states: In oxidized thioredoxin, the cysteine residues are linked to form a disulfide bridge , and there are two reduced SH groups in the enzyme.
Individual evidence
- ↑ Swiss Institute of Bioinformatics (SIB): PROSITE documentation PDOC0172. Thioredoxin family. Retrieved August 12, 2011 .
- ↑ Thioredoxin. In: Online Mendelian Inheritance in Man . (English)