Hsp33

InterPro Family
Hsp33 protein
Identifiers
SymbolHsp33
PfamPF01430
InterProIPR000397
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDBPDB: 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

  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.
  • v
  • t
  • e
Posttranslational modification
Chaperones/
protein folding
Heat shock proteins/
Chaperonins
  • Hsp10/GroES
  • Hsp27
  • Hsp47
  • HSP60/GroEL
Other
Protein targetingUbiquitin
(ubiquitylation)Ubiquitin-like proteins
(UBL)
SUMO protein
(SUMOylation)
  • E1 SUMO-activating enzyme
  • E2 SUMO-conjugating enzyme
Other
This article incorporates text from the public domain Pfam and InterPro: IPR000397