Hsp33

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

Hsp33 protein
Hsp33 protein
Identifiers
Symbol	Hsp33
Pfam	PF01430
InterPro	IPR000397
Pfam
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

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]

References[edit]

^ Jakob U, Muse W, Eser M, Bardwell JC (1999). "Chaperone activity with a redox switch". Cell. 96 (3): 341–352. doi:10.1016/S0092-8674(00)80547-4. PMID 10025400.

This article incorporates text from the public domain Pfam and InterPro: IPR000397

[PUB00000967-1] Jakob U, Muse W, Eser M, Bardwell JC (1999). "Chaperone activity with a redox switch". Cell. 96 (3): 341–352. doi:10.1016/S0092-8674(00)80547-4. PMID 10025400.

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