Belfield WJ

Cole DJ

Dunn SMJ

Holt A

Kozuska JL

Martin IL

Paulsen IM

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

Impact of Intracellular Domain Flexibility upon Properties of Activated Human 5-HT<sub>3</sub> Receptors

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