Regulation of a pentameric ligand-gated ion channel by a semiconserved cationic lipid-binding site.

ABSTRACT: Pentameric ligand-gated ion channels (pLGICs) are crucial mediators of electrochemical signal transduction in various organisms from bacteria to humans. Lipids play an important role in regulating pLGIC function, yet the structural bases for specific pLGIC-lipid interactions remain poorly understood. The bacterial channel ELIC recapitulates several properties of eukaryotic pLGICs, including activation by the neurotransmitter GABA and binding and modulation by lipids, offering a simplified model system for structure-function relationship studies. In this study, functional effects of noncanonical amino acid substitution of a potential lipid-interacting residue (W206) at the top of the M1-helix, combined with detergent interactions observed in recent X-ray structures, are consistent with this

SUBMITTER: Sridhar A 

PROVIDER: S-EPMC8327344 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature