Open AccessComputer modelling of the transmembrane channel formed by a CNBr peptide of diphtheria toxin B fragment
Author(s) -
Cabiaux V.,
Brasseur R.,
Mindell J.,
Ruysschaert J.M.
Publication year - 1992
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1992.tb05893.x
Subject(s) - diphtheria toxin , peptide , chemistry , bilayer , cyanogen bromide , toxin , amphiphile , lipid bilayer , transmembrane protein , biophysics , stereochemistry , biochemistry , peptide sequence , membrane , biology , receptor , organic chemistry , copolymer , gene , polymer
Diphtheria toxin (DT) forms transmembrane, voltage‐dependent channels in a planar lipid bilayer. Channels with similar characteristics were obtained with CB1, a cyanogen bromide peptide of diphtheria toxin B fragment (DTB) (res 340–459). Tryptophan 398 is in interaction with the hydrophobic core of the lipid bilayer. Using the Eisenberg method in association with the Shiffer‐Edmunson wheel representation, we have identified two amphipathic α‐helices within CB1 (res 346–364 and 389–406) that could be involved in the interaction with lipids. Bearing this information in mind, we are providing a model for the structure of the CB1 channel.