Probing the structure of the diphtheria toxin channel. Reactivity in planar lipid bilayer membranes of cysteine-substituted mutant channels with methanethiosulfonate derivatives.

doi:10.1085/jgp.110.3.229

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Article

Probing the structure of the diphtheria toxin channel. Reactivity in planar lipid bilayer membranes of cysteine-substituted mutant channels with methanethiosulfonate derivatives.

The Journal of general physiology - 1 Sept 1997

Huynh P D, Cui C, Zhan H, Oh K J, Collier R J, Finkelstein A

Abstract excerpt

Previous work has established that the 61 amino acid stretch from residue 322 to 382 in the T-domain of diphtheria toxin forms channels indistinguishable in ion-conducting properties from those formed by the entire T-domain. In the crystal structure of the toxin's water-soluble form, the bulk of...

Topics

Amino Acid Sequence
Cysteine
Diphtheria Toxin
Ion Channels
Lipid Bilayers
Mesylates
Mutation
Stereoisomerism
Thiosulfonic Acids

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