Article
Topography of helices 5-7 in membrane-inserted diphtheria toxin T domain: identification and insertion boundaries of two hydrophobic sequences that do not form a stable transmembrane hairpin.
The Journal of biological chemistry - 10 May 2002
Rosconi Michael P, London Erwin
Abstract excerpt
The T domain of diphtheria toxin undergoes a low pH-induced conformational change that allows it to penetrate cell membranes. T domain hydrophobic helices 8 and 9 can adopt two conformations, one close to the membrane surface (P state) and a second in which they apparently form a transmembrane hairpin (TM state). We have now studied T domain helices 5-7, a second cluster of hydrophobic helices, using Cys-scanning...
Topics
- Amino Acid Sequence
- Boron Compounds
- Bridged Bicyclo Compounds, Heterocyclic
- Cell Membrane
- Circular Dichroism
- Cysteine
- Diphtheria Toxin
- Escherichia coli
- Fluorescent Dyes
- Hydrogen-Ion Concentration
- Lipid Bilayers
- Models, Biological
- Molecular Sequence Data