| Primary Identifier | IPR037913 | Type | Domain |
| Short Name | ACD_IbpA/B |
| description | This is the alpha-crystallin domain (ACD) found in Escherichia coli inclusion body-associated proteins IbpA and IbpB, and similar proteins. This domain is also found in class A small heat shock proteins from Bradyrhizobium, which consists of proteins that show similarity to E. coli IbpA and IbpB [].IbpA and IbpB are 16kDa small heat shock proteins (sHsps). sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. They all contain a conserved alpha-crystallin domain flanked by variable N- and C-terminal tails []. IbpA and IbpB are produced during high-level production of various heterologous proteins, specifically human prorenin, renin and bovine insulin-like growth factor 2 (bIGF-2), and are strongly associated with inclusion bodies containing these heterologous proteins []. IbpA and IbpB work as an integrated system to stabilize thermally aggregated proteins in a disaggregation competent state []. The chaperone activity of IbpB is also significantly elevated as the temperature increases from normal to heat shock. The high temperature results in the disassociation of 2-3-MDa IbpB oligomers into smaller approximately 600kDa structures. This elevated activity seen under heat shock conditions is retained for an extended period of time after the temperature is returned to normal []. IbpA also forms multimers []. |
