Insertion and organization within membranes of the δ-endotoxin pore-forming domain, helix 4-loop-helix 5, and inhibition of its activity by a mutant helix 4 peptide
D Gerber, Y Shai - Journal of Biological Chemistry, 2000 - ASBMB
The pore-forming domain of Bacillus thuringiensis Cry1Ac insecticidal protein comprises of a
seven α-helix bundle (α1–α7). According to the" umbrella model," α4 and α5 helices form a
hairpin structure thought to be inserted into the membrane upon binding. Here, we have
synthesized and characterized the hairpin domain, α4-loop-α5, its α4 and α5 helices, as well
as mutant α4 peptides based on mutations that increased or decreased toxin toxicity.
Membrane permeation studies revealed that the α4-loop-α5 hairpin is extremely active …
seven α-helix bundle (α1–α7). According to the" umbrella model," α4 and α5 helices form a
hairpin structure thought to be inserted into the membrane upon binding. Here, we have
synthesized and characterized the hairpin domain, α4-loop-α5, its α4 and α5 helices, as well
as mutant α4 peptides based on mutations that increased or decreased toxin toxicity.
Membrane permeation studies revealed that the α4-loop-α5 hairpin is extremely active …
