A triad of residues is functionally transferrable between 5-HT₃ serotonin receptors and nicotinic acetylcholine receptors.

ABSTRACT: Cys-loop receptors are pentameric ligand-gated ion channels that facilitate communication within the nervous system. Upon neurotransmitter binding, these receptors undergo an allosteric activation mechanism connecting the binding event to the membrane-spanning channel pore, which expands to conduct ions. Some of the earliest steps in this activation mechanism are carried out by residues proximal to the binding site, the relative positioning of which may reflect functional differences among members of the Cys-loop family of receptors. Herein, we investigated key side-chain interactions near the binding site via mutagenesis and two-electrode voltage-clamp electrophysiology in serotonin-gated 5-HT_3A receptors (5-HT_3ARs) and nicotinic acetylcholine receptors (nAChRs) expr

SUBMITTER: Mosesso R 

PROVIDER: S-EPMC5827437 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature