Alpha-crystallin domain (ACD) of alpha-crystallin-type small(s) heat shock proteins (Hsps). sHsps are small stress induced proteins with monomeric masses between 12 -43 kDa, whose common feature is the Alpha-crystallin domain (ACD). sHsps are generally active as large oligomers consisting of multiple subunits, and are believed to be ATP-independent chaperones that prevent aggregation and are important in refolding in combination with other Hsps.
Structure:2H50, Saccharomyces cerevisiae Hsp26 dimer interface, contacts at 3.5 A
Comment:ScHsp26 assembles in shell-like particles composed of 24 subunits. These particles are storage forms which upon heat shock disassociate into dimers. Non-native substrate proteins bind the disassociated ScHsp26 and assemble into large globular assemblies having one monomer of substrate bound per dimer.
Structure:1GME_A, Triticum aestivum sHsp dimer interface, contacts at 3.5 A
Comment:T. aestivum HSP16.9 assembles as a 12-mer, comprised of two discs, each disc having 6 alpha crystallin-like domains organized as a trimer of dimers.
Jiyao W et al.(2023). "The conserved domain database in 2023.",