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Article

Structure-function relationships in diphtheria toxin channels: III. Residues which affect the cis pH dependence of channel conductance.

The Journal of membrane biology - 1 Jan 1994

Mindell J A, Silverman J A, Collier R J, Finkelstein A

Abstract excerpt

The conductance of channels formed by diphtheria toxin (DT) in lipid bilayer membrane depends strongly on pH. We have previously shown that a 61 amino acid region of the protein, denoted TH8-9, is sufficient to form channels having the same pH-dependent conductance properties as those of whole toxin channels. One residue in this region, Aspartate 352, is responsible for all the dependence of single channel...

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Identifiers

PMID: 7516434
DOI: 10.1007/BF00234997

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Structure-function relationships in diphtheria toxin channels: III. Residues which affect the cis pH dependence of channel conductance.PMID 7516434Read ↗

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

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pH-dependent insertion of proteins into membranes: B-chain mutation of diphtheria toxin that inhibits membrane translocation, Glu-349----Lys.Semantic proximity Read ↗

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