Protein engineering of Bacillus thuringiensis δ-endotoxin: Mutations at domain II of CryIAb enhance receptor affinity and toxicity toward gypsy moth larvae

Substitutions or deletions of domain II loop residues of Bacillus thuringiensis δ-endotoxin CryIAb were constructed using site-directed mutagenesis techniques to investigate their functional roles in receptor binding and toxicity toward gypsy moth (Lymantria dispar). Substitution of loop 2 residue N...

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Bibliografische gegevens

Gepubliceerd in:	Proc Natl Acad Sci U S A
Hoofdauteurs:	Rajamohan, Francis, Alzate, Oscar, Cotrill, Jeffrey A., Curtiss, April, Dean, Donald H.
Formaat:	Artigo
Taal:	Inglês
Gepubliceerd in:	National Academy of Sciences 1996
Onderwerpen:	Biological Sciences
Online toegang:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC26133/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8962052/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.93.25.14338
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