{{Short description|InterPro Family}} {{Pfam box |Symbol = Hsp33 |Name = Hsp33 protein |Pfam = PF01430 |InterPro = IPR000397 |PROSITE = |PDB = {{PDB|1hw7}} {{PDB|1i7f}} {{PDB|1vq0}} {{PDB|1vzy}} {{PDB|1xjh}} }}
'''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 H<sub>2</sub>O<sub>2</sub> cause disulphide bonds to form in Hsp33, a process that leads to the activation of its chaperone function.<ref name="PUB00000967">{{cite journal |vauthors=Jakob U, Muse W, Eser M, Bardwell JC |title=Chaperone activity with a redox switch |journal=Cell |volume=96 |issue=3 |pages=341–352 |year=1999 |pmid=10025400 |doi=10.1016/S0092-8674(00)80547-4|doi-access=free }}</ref>
==References== {{reflist}} {{Chaperones}}
{{InterPro content|IPR000397}}
Category:Heat shock proteins Category:Molecular chaperones