Protein Family Models

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. Oxidising conditions like H2O2 cause disulfide bonds to form in Hsp33, a process that leads to the activation of its chaperone function [1]. [1]. 10025400. Chaperone activity with a redox switch. Jakob U, Muse W, Eser M, Bardwell JC;. Cell 1999;96:341-352. [2]. 11377197. The 2.2 A crystal structure of Hsp33: a heat shock protein with redox-regulated chaperone activity. Vijayalakshmi J, Mukhergee MK, Graumann J, Jakob U, Saper MA;. Structure (Camb) 2001;9:367-375. (from Pfam)

Date:

2024-10-16

Gene:

hslO

Date:

2021-07-23

Hsp33 family molecular chaperone HslO is redox regulated and protects both thermally-unfolding and oxidatively-damaged proteins from irreversible aggregation

Date:

2023-02-22