| Hsp33 protein | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||||
| Symbol | Hsp33 | ||||||||||
| Pfam | PF01430 | ||||||||||
| InterPro | IPR000397 | ||||||||||
| |||||||||||
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
- ^ 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.
| Hsp33 protein | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||||
| Symbol | Hsp33 | ||||||||||
| Pfam | PF01430 | ||||||||||
| InterPro | IPR000397 | ||||||||||
| |||||||||||
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
- ^ 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.