InterPro domain: IPR016154

This superfamily represents the C-terminal alpha/beta domain from the heat shock protein Hsp33. Hsp33 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 localised protein with highly reactive cysteines that respond quickly to changes in the redox environment. Oxidizing conditions like H ₂ O ₂ cause disulphide bonds to form in Hsp33, a process that leads to the activation of its chaperone function [ 1 ].

1. Chaperone activity with a redox switch. Cell 96, 341-52