A combination of molecular dynamics simulations and electron cryomicroscopy characterizes interactions of a pentameric ligand-gated ion channel with 25 lipid molecules, specifically in a functional state in which they were not previously observed.

Computational models of gating processes in an ion channel show how stability shifts upon ligand-binding and mutations are reproduced, which highlights mechanistic details and proposes a new role for symmetry in gating.

Development of nanobodies against a model pentameric ligand-gated ion channel demonstrates they can be functionally active as negative or positive allosteric modulators and offers opportunities for future drug development.

Polyunsaturated fatty acids enhance desensitization in pentameric ligand-gated ion channels.

Docosahexaenoic acid (DHA) inhibits ELIC through state-dependent binding to a single site.

Phosphatidylglycerol binding at multiple sites stabilizes the open state relative to the desensitized state of a pentameric ligand-gated ion channel.

Structural and functional studies of a potassium ion channel that is opened and closed by different ligands have revealed a novel gating mechanism.

Cryo-EM structures of Cys-loop receptor Alpo4 from the thermophilic worm Alvinella pompejana show that a sterol derivative CHAPS binds in and outside of its orthosteric binding site and induces a quaternary twist.

Allosteric reorganizations of a bacterial channel receptor are mapped along the protein structure, using the site-directed bimane quenching fluorescence technique, through parallel real-time conformational and electrophysiological recordings.

High resolution SthK channel cryo-EM structures in different ligand-bound states combined with single-channel functional data in the same conditions constrain a gating mechanism for CNG channels.