Role of Interdomain Salt Bridges in the Pore-forming Ability of the Bacillus thuringiensis Toxins Cry1Aa and Cry1Ac
Open Access
- 1 September 2001
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 276 (38) , 35546-35551
- https://doi.org/10.1074/jbc.m101887200
Abstract
No abstract availableKeywords
This publication has 62 references indexed in Scilit:
- 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 toxinJournal of Molecular Biology, 1999
- SWISS‐MODEL and the Swiss‐Pdb Viewer: An environment for comparative protein modelingElectrophoresis, 1997
- Involvement of Two Amino Acid Residues in the Loop Region ofBacillus thuringiensisCry1Ab Toxin in Toxicity and Binding toLymantria disparBiochemical and Biophysical Research Communications, 1996
- Functional Significance of Loops in The Receptor Binding Domain ofBacillus thuringiensisCryIIIA δ-EndotoxinJournal of Molecular Biology, 1996
- Bacillus thuringiensisCrylA(a) Insecticidal Toxin: Crystal Structure and Channel FormationJournal of Molecular Biology, 1995
- Domain-III Exchanges of Bacillus thuringiensisCryIA Toxins Affect Binding to Different Gypsy Moth Midgut ReceptorsBiochemical and Biophysical Research Communications, 1995
- Ion Channel Activity of N-Terminal Fragments from CryIA(c) Delta-EndotoxinBiochemical and Biophysical Research Communications, 1993
- Structural and functional characterization of the .alpha.5 segment of Bacillus thuringiensis .delta.-endotoxinBiochemistry, 1993
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Maturation of the head of bacteriophage T4Journal of Molecular Biology, 1973