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Impact of intracellular domain flexibility upon properties of activated human 5‐ HT 3 receptors
Author(s) -
Kozuska J L,
Paulsen I M,
Belfield W J,
Martin I L,
Cole D J,
Holt A,
Dunn S M J
Publication year - 2014
Publication title -
british journal of pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1111/bph.12536
Subject(s) - homomeric , intracellular , receptor , mutant , biophysics , microbiology and biotechnology , chemistry , gating , wild type , g protein coupled receptor , arginine , biology , biochemistry , amino acid , protein subunit , gene
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 homomer may impart structural rigidity, and we hypothesized that this rigidity could account for the low conductance.