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.

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

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.

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

Ion conduction in the calcium-activated chloride channel TMEM16A is directly regulated by calcium, which binds to a site close to the pore thereby shaping the electrostatics at its intracellular entrance.

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.

The K(+) uptake system KtrAB is controlled by an allosteric mechanism entirely new for membrane channels, which operates the channel gate over a 35 Å distance.

Ligand-induced two-fold symmetric arrangement in TRPV2 is observed in the native-like nanodisc-reconstituted condition using cryo-electron microscopy.

Comparative genomics and three-dimensional protein modelling identify homologs of insect chemosensory receptors in unicellular eukaryotes and plants.