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Article

Impact of intracellular domain flexibility upon properties of activated human 5-HT3 receptors.

British journal of pharmacology - 1 Apr 2014

Kozuska J L, Paulsen I M, Belfield W J, Martin I L, Cole D J, Holt A, Dunn S M J

Abstract excerpt

BACKGROUND AND PURPOSE: It has been proposed that arginine residues lining the intracellular portals of the homomeric 5-HT3 A receptor cause electrostatic repulsion of cation flow, accounting for a single-channel conductance substantially lower than that of the 5-HT3 AB heteromer. However, comparison of receptor homology models for wild-type pentamers suggests that salt bridges in the intracellular domain of the...

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Source

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Identifiers

PMID: 24283776
DOI: 10.1111/bph.12536
PMCID: PMC3966743

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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