Amino acids Y229 and F603 are involved in Bacillus thuringiensis Cry1Ac δ-endotoxin stability and toxicity
Author:
Affiliation:
1. Biopesticides team (LPAP)
2. Laboratory of Microorganismes and Biomolecules; Centre of Biotechnology of Sfax; University of Sfax; Sfax; Tunisia
Publisher
Oxford University Press (OUP)
Subject
Genetics,Molecular Biology,Microbiology
Link
http://academic.oup.com/femsle/article-pdf/329/1/54/19124656/329-1-54.pdf
Reference32 articles.
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3. Immunocytochemical analysis of specific binding of Bacillus thuringiensis insecticidal crystal proteins to lepidopteran and coleopteran midgut membranes;Bravo;J Invertebr Pathol,1992
4. N-acetylgalactosamine on the putative insect receptor aminopeptidase N is recognised by a site on the domain III lectin-like fold of a Bacillus thuringiensis insecticidal toxin;Burton;J Mol Biol,1999
5. Amino acid substitution in alpha-helix 7 of Cry1Ac δ-endotoxin of Bacillus thuringiensis leads to enhanced toxicity to Helicoverpa armigera Hubner;Chandra;FEBS Lett,1999
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5. His180 in the pore-lining α4 of the Bacillus thuringiensis Cry4Aa δ-endotoxin is crucial for structural arrangements of the α4-α5 transmembrane hairpin and hence biotoxicity;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2021-06
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