InterPro domain: IPR031107

Prokaryotic and eukaryotic organisms respond to heat shock or otherenvironmental stress by inducing the synthesis of proteins collectively knownas heat-shock proteins (hsp) [ 1 ]. Amongst them is a family of proteins with an average molecular weight of 20 Kd, known as the hsp20 proteins [ 2 , 3 , 4 ]. These seem to act as chaperones that can protect other proteins against heat-induced denaturation and aggregation. Hsp20 proteins seem to form large heterooligomeric aggregates.

Structurally, this family is characterised by the presence of a conserved C-terminal domain of about 100 residues.

This family also includes the related alpha-crystallin (alphaC) protein [ 5 ].

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1. The heat-shock proteins. Annu. Rev. Genet. 22, 631-77
2. The expanding small heat-shock protein family, and structure predictions of the conserved "alpha-crystallin domain". J. Mol. Evol. 40, 238-48
3. Protein folding: junior chaperones. Curr. Biol. 3, 234-5
4. Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones. Trends Biochem. Sci. 19, 205-11
5. Small heat shock proteins and α-crystallins: dynamic proteins with flexible functions. Trends Biochem. Sci. 37, 106-17