Bivalent sequential binding model of a Bacillus thuringiensis toxin to gypsy moth aminopeptidase N receptor.

@article{Jenkins2000BivalentSB,
  title={Bivalent sequential binding model of a Bacillus thuringiensis toxin to gypsy moth aminopeptidase N receptor.},
  author={Jeremy L. Jenkins and Mi Kyong Lee and Algimantas P. Valaitis and Ashley Brian Sockwell Curtiss and Donald Harry Dean},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 19},
  pages={
          14423-31
        }
}
Specificity for target insects of Bacillus thuringiensis insecticidal Cry toxins is largely determined by toxin affinity for insect midgut receptors. The mode of binding for one such toxin-receptor complex was investigated by extensive toxin mutagenesis, followed by real-time receptor binding analysis using an optical biosensor (BIAcore). Wild-type Cry1Ac, a three-domain, lepidopteran-specific toxin, bound purified gypsy moth (Lymantria dispar) aminopeptidase N (APN) biphasically. Site 1… CONTINUE READING
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