| Description | This entry represents the conserved second domain of the toxic core.The crystal proteins of Bacillus thuringiensis have been extensively studied because of their pesticidal properties and their high natural levels of production [ ]. 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 () involved in membrane insertion and pore formation; a β-sheet central domain involved in receptor binding; and a C-terminal β-sandwich domain ( ) that interacts with the N-terminal domain to form a channel [ , ].This entry represents the central β-sheet domain, which consists of three four-stranded β-sheets, each with a Greek key fold, with internal pseudo threefold symmetry. Thus, it acts as a receptor binding β-prism, binding to insect-specific receptors of gut epithelial cells [ ]. | Name | Pesticidal crystal protein, domain II |
| Short Name | Pest_cryst_dom_II | Type | Domain |
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