| Description | 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 localized protein with highly reactive cysteines that respond quickly to changes in the redox environment. Oxidizing conditions like H 2O 2cause disulphide bonds to form in Hsp33, a process that leads to the activation of its chaperone function. In normal (reducing) cytosolic conditions, four conserved Cys residues are coordinated by a Zn ion. Hsp33 is homodimeric in its functional form [ , , , ].This superfamily represents a helix hairpin bin domain found in Hsp33. This domain folds into three helices that pack on the other subunit of the Hsp33 dimer []. | Name | Heat shock protein Hsp33, helix hairpin bin domain superfamily |
| Short Name | Hsp33_helix_hairpin_bin_dom_sf | Type | Homologous_superfamily |
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