Colleen M. Noviello

TL;DR: The cryo-electron microscopy structure of the type A GABA receptor bound to GABA and the benzodiazepine site antagonist flumazenil reveals structural mechanisms that underlie intersubunit interactions and ligand selectivity of the receptor.

TL;DR: This X-ray crystallographic structure of the human α4β2 nicotinic receptor provides insights into the architectural principles governing ligand recognition, heteromer assembly, ion permeation and desensitization in this prototypical receptor class.

TL;DR: Cryo-electron microscopy structures of GABA A receptors bound to intravenous anaesthetic and benzodiazepines reveal both common and distinct transmembrane binding sites, and show that the mechanisms of action of anaesthetics partially overlap with those of benzodiazines.

TL;DR: The first high-resolution structure of the receptor type found in muscle-endplate membrane and in the muscle-derived electric tissues of fish is presented, providing a framework for understanding gating in ligand-gated channels and how mutations in the acetylcholine receptor cause congenital myasthenic syndromes.

TL;DR: The structures of the α3β4 nicotinic receptor in lipidic and detergent environments are presented, using functional reconstitution to define lipids appropriate for structural analysis and suggest principles of agonist selectivity.