Impact of intracellular domain flexibility upon properties of activated human 5‐ HT  3  receptors | Zendy

Kozuska J L | Zendy; Paulsen I M | Zendy; Belfield W J | Zendy; Martin I L | Zendy; Cole D J | Zendy; Holt A | Zendy; Dunn S M J | Zendy

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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.

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