| Description | This superfamily represents the N-terminal, 3-layer β/α/β 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 2O 2cause disulphide bonds to form in Hsp33, a process that leads to the activation of its chaperone function [ ]. | Name | Heat shock protein Hsp33, N-terminal |
| Short Name | Heat_shock_Hsp33_N | Type | Homologous_superfamily |
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