Article
Structure-function relationships in diphtheria toxin channels: I. Determining a minimal channel-forming domain.
The Journal of membrane biology - 1 Jan 1994
Silverman J A, Mindell J A, Zhan H, Finkelstein A, Collier R J
Abstract excerpt
Diphtheria Toxin (DT) is a 535 amino acid exotoxin, whose active form consists of two polypeptide chains linked by an interchain disulphide bond. DT's N-terminal A fragment kills cells by enzymatically inactivating their protein synthetic machinery; its C-terminal B chain is required for the binding of toxin to sensitive cells and for the translocation of the A fragment into the cytosol. This B fragment,...
Topics
- Amino Acid Sequence
- Diphtheria Toxin
- Hydrogen-Ion Concentration
- Interleukin-2
- Ion Channels
- Lipid Bilayers
- Membrane Potentials
- Membranes, Artificial
- Molecular Sequence Data
- Mutation
- Structure-Activity Relationship