Hsp33

Hsp33 protein
Identifiers
SymbolHsp33
PfamPF01430
InterProIPR000397
Available protein structures:
PDB  PDB: 1hw7​ PDB: 1i7f​ PDB: 1vq0​ PDB: 1vzy​ PDB: 1xjh​ IPR000397 PF01430 (ECOD; PDBsum)  
AlphaFold

Hsp33 protein is a molecular chaperone, distinguished from all other known chaperones by its mode of functional regulation. Its activity is redox regulated. Hsp33 is a cytoplasmically localized protein with highly reactive cysteines that respond quickly to changes in the redox environment. Oxidizing conditions like H2O2 cause disulphide bonds to form in Hsp33, a process that leads to the activation of its chaperone function.[1]

References

  1. ^ Jakob U, Muse W, Eser M, Bardwell JC (1999). "Chaperone activity with a redox switch". Cell. 96 (3): 341–352. doi:10.1016/S0092-8674(00)80547-4. PMID 10025400.
This article incorporates text from the public domain Pfam and InterPro: IPR000397

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