Hsp20
| Hsp20/alpha crystallin family | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | HSP20 | ||||||||
| Pfam | PF00011 | ||||||||
| InterPro | IPR002068 | ||||||||
| PROSITE | PDOC00791 | ||||||||
| SCOP | 1shs | ||||||||
| SUPERFAMILY | 1shs | ||||||||
| CDD | cd06464 | ||||||||
| |||||||||
Heat shock protein Hsp20 is a family of heat shock proteins.
Prokaryotic and eukaryotic organisms respond to heat shock or other environmental stress by inducing the synthesis of proteins collectively known as 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] These seem to act as protein 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, alpha-crystallin domain, of about 100 residues. Recently, small heat shock proteins (sHSPs) were found in marine viruses (cyanophages).[3]
Human proteins containing this domain
CRYAA; CRYAB; HSPB1; HSPB2; HSPB3; HSPB6; HSPB7; HSPB8; HSPB9;
References
- ↑ Lindquist S, Craig EA (1988). "The heat-shock proteins". Annu. Rev. Genet. 22: 631–677. doi:10.1146/annurev.ge.22.120188.003215. PMID 2853609.
- ↑ Merck KB, de Jong WW, Bloemendal H, Groenen PJ (1994). "Structure and modifications of the junior chaperone alpha-crystallin. From lens transparency to molecular pathology". Eur. J. Biochem. 225 (1): 1–9. doi:10.1111/j.1432-1033.1994.00001.x. PMID 7925426.
- ↑ Maaroufi H, Tanguay RM (2013). "Analysis and phylogeny of small heat shock proteins from marine viruses and their cyanobacteria host.". PLoS ONE 8 (11): e81207. doi:10.1371/journal.pone.0081207. PMC 3827213. PMID 24265841.
This article incorporates text from the public domain Pfam and InterPro IPR002068