Homologous Superfamily

Heat shock protein Hsp33, helix hairpin bin domain superfamily (IPR023212)

Short name: Hsp33_helix_hairpin_bin_dom_sf

Overlapping entries


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 H2O2 cause 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 [PMID: 10025400, PMID: 11323724, PMID: 10102262, PMID: 10359689].

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 [PMID: 11377197].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.