Biology:Hsp33

From HandWiki
Short description: InterPro Family
Hsp33 protein
Identifiers
SymbolHsp33
PfamPF01430
InterProIPR000397

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. "Chaperone activity with a redox switch". Cell 96 (3): 341–352. 1999. doi:10.1016/S0092-8674(00)80547-4. PMID 10025400. 
This article incorporates text from the public domain Pfam and InterPro: IPR000397