Hsp33

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]

Hsp33 protein
Identifiers
Symbol	Hsp33
Pfam	PF01430
InterPro	IPR000397
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary PDB PDB: 1hw7​ PDB: 1i7f​ PDB: 1vq0​ PDB: 1vzy​ PDB: 1xjh​