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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,...

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Identifiers

PMID: 7516432
DOI: 10.1007/BF00234995

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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: I. Determining a minimal channel-forming domain.PMID 7516432Read ↗

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

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Structures of distant diphtheria toxin homologs reveal functional determinants of an evolutionarily conserved toxin scaffoldSemantic proximity Read ↗

Behavior of the deeply inserted helices in diphtheria toxin T domain: helices 5, 8, and 9 interact strongly and promote pore formation, while helices 6/7 limit pore formation.Semantic proximity Read ↗

Structure/function analysis of interleukin-2-toxin (DAB486-IL-2). Fragment B sequences required for the delivery of fragment A to the cytosol of target cells.Semantic proximity Read ↗

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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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