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Impact of Intracellular Domain Flexibility upon Properties of Activated Human 5-HT3 Receptors

Lookup NU author(s): Dr Daniel ColeORCiD



This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License (CC BY-NC 4.0).


It has been proposed that arginine residues lining the intracellular portals of the homomeric 5-HT3A receptor cause electrostatic repulsion of cation flow, accounting for a single-channel conductance substantially lower than that of the 5-HT3AB heteromer. However, comparison of receptor homology models for wild-type pentamers suggests that salt bridges in the intracellular domain of the homomer may impart structural rigidity, and we hypothesized that this rigidity could account for the low conductance.

Publication metadata

Author(s): Kozuska JL, Paulsen IM, Belfield WJ, Martin IL, Cole DJ, Holt A, Dunn SMJ

Publication type: Article

Publication status: Published

Journal: British Journal of Pharmacology

Year: 2014

Volume: 171

Issue: 7

Pages: 1617-1628

Print publication date: 01/04/2014

Online publication date: 18/03/2014

Acceptance date: 18/03/2014

Date deposited: 19/09/2016

ISSN (print): 0007-1188

ISSN (electronic): 1476-5381

Publisher: Wiley-Blackwell


DOI: 10.1111/bph.12536


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