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Article

Role of acidic residues in helices TH8-TH9 in membrane interactions of the diphtheria toxin T domain.

Toxins - 14 Apr 2015

Ghatak Chiranjib, Rodnin Mykola V, Vargas-Uribe Mauricio, McCluskey Andrew J, Flores-Canales Jose C, Kurnikova Maria, Ladokhin Alexey S

Abstract excerpt

The pH-triggered membrane insertion of the diphtheria toxin translocation domain (T domain) results in transferring the catalytic domain into the cytosol, which is relevant to potential biomedical applications as a cargo-delivery system. Protonation of residues is suggested to play a key role in the process, and residues E349, D352 and E362 are of particular interest because of their location within the membrane...

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Identifiers

PMID: 25875295
DOI: 10.3390/toxins7041303
PMCID: PMC4417968

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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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Role of acidic residues in helices TH8-TH9 in membrane interactions of the diphtheria toxin T domain.PMID 25875295Read ↗

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