Homologous Superfamily

Pesticidal crystal protein, central domain superfamily (IPR036399)

Short name: Pest_cryst_cen_dom_sf

Overlapping entries


The crystal proteins of Bacillus thuringiensis have been extensively studied because of their pesticidal properties and their high natural levels of production [PMID: 9729610]. When an insect ingests these proteins, they are activated by proteolytic cleavage. The N terminus is cleaved in all of the proteins and a C-terminal extension is cleaved in some members. Once activated, the endotoxin binds to the gut epithelium and causes cell lysis by the formation of cation-selective channels, which leads to death. The activated region of the toxin is composed of three distinct structural domains: an N-terminal helical bundle domain (IPR005639) involved in membrane insertion and pore formation; a beta-sheet central domain involved in receptor binding; and a C-terminal beta-sandwich domain (IPR005638) that interacts with the N-terminal domain to form a channel [PMID: 7490762, PMID: 11468393].

This entry represents the central beta-sheet domain superfamily, which consists of three four-stranded beta-sheets, each with a Greek key fold, with internal pseudo threefold symmetry. Thus, it acts as a receptor binding beta-prism, binding to insect-specific receptors of gut epithelial cells [PMID: 11377201].

GO terms

Biological Process

GO:0009405 pathogenesis

Molecular Function

GO:0005102 signaling receptor binding

Cellular Component

No terms assigned in this category.

Contributing signatures

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