Protein Family Models for Protein (Select 446579028) - Protein Family Models

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Items: 6

Select item 4121691.

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)

GO Terms:

Cellular Component:: cytoplasm (GO:0005737)

Biological Process:: protein folding (GO:0006457)

Molecular Function:: unfolded protein binding (GO:0051082)

Date:: 2024-10-16

Family Accession:: NF013589.5
Method:: HMM

Select item 3895952.

new record, indexing in progress

Family Accession:

Select item 3471773.

new record, indexing in progress

Family Accession:

Select item 1927204.

redox-regulated molecular chaperone HslO

Gene:: hslO

Date:: 2018-10-02

Family Accession:: NBR006801
Method:: BlastRule

Select item 1710105.

Hsp33 family molecular chaperone HslO

Gene:: hslO

GO Terms:

Biological Process:: protein folding (GO:0006457)

Molecular Function:: unfolded protein binding (GO:0051082)

Date:: 2021-07-23

Family Accession:: NF001033.0
Method:: HMM

Select item 598616.

Hsp33 family molecular chaperone HslO

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