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