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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.
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
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
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