Computer modelling of the transmembrane channel formed by a CNBr peptide of diphtheria toxin B fragment.
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 alpha-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.
Cabiaux
V
V
Laboratoire des Macromolécules aux Interfaces, Université Libre de Bruxelles, Belgium.
Brasseur
R
R
Mindell
J
J
Ruysschaert
J M
JM
D000595:Amino Acid Sequence; D003198:Computer Simulation; D004167:Diphtheria Toxin / Q000737:chemistry* / Q000633:toxicity; D005453:Fluorescence; D007473:Ion Channels / Q000187:drug effects*; D008051:Lipid Bilayers; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000633:toxicity; D011487:Protein Conformation
D004167:Diphtheria Toxin; D007473:Ion Channels; D008051:Lipid Bilayers; D010446:Peptide Fragments; C039171:diphtheria toxin fragment B