title: Ionotropic glutamate receptors made crystal clear.
abstract: Two recent crystallographic studies of the full-length GluA2 AMPA receptor provide our first insights into how the modular domains of the tetrameric complex coordinate the process of activation. These findings herald a new era in the structure-function analyses of neurotransmitter receptors, a fitting achievement for the 'International Year of Crystallography'.
authors.affiliation: Department of Pharmacology and Therapeutics, McGill University, Montréal, Québec, Canada. Electronic address: derek.bowie@mcgill.ca.
authors.forename: Derek
authors.initials: D
authors.lastname: Bowie
mesh_terms: D006801:Humans; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D018091:Receptors, AMPA / Q000378:metabolism*; D058468:Receptors, Ionotropic Glutamate / Q000737:chemistry* / Q000378:metabolism; D017981:Receptors, Neurotransmitter / Q000737:chemistry* / Q000378:metabolism
chemical_list: D018091:Receptors, AMPA; D058468:Receptors, Ionotropic Glutamate; D017981:Receptors, Neurotransmitter; C104722:glutamate receptor ionotropic, AMPA 2