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Literature summary for 3.4.11.2 extracted from

  • Gomez, I.; Arenas, I.; Benitez, I.; Miranda-Rios, J.; Becerril, B.; Grande, R.; Almagro, J.C.; Bravo, A.; Soberon, M.
    Specific epitopes of domains II and III of Bacillus thuringiensis Cry1Ab toxin involved in the sequential interaction with cadherin and aminopeptidase-N receptors in Manduca sexta (2006), J. Biol. Chem., 281, 34032-34039.
    View publication on PubMed

Application

Application Comment Organism
medicine Bacillus thuringiensis Cry1Ab toxin binds to cadherin through loops 2 and 3 of domain II promoting the formation of the pre-pore inducing some structural changes, then the pre-pore interacts with aminopeptidese N through beta-16 of domain III promoting membrane insertion of the toxin and cell death Manduca sexta

Organism

Organism UniProt Comment Textmining
Manduca sexta
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Subunits

Subunits Comment Organism
More Bacillus thuringiensis Cry1Ab toxin binds to cadherin through loops 2 and 3 of domain II promoting the formation of the pre-pore inducing some structural changes, then the pre-pore interacts with aminopeptidese N through beta-16 of domain III promoting membrane insertion of the toxin and cell death Manduca sexta