title: Glutamate receptor gating.
abstract: Ionotropic glutamate receptors (iGluRs) mediate the vast majority of fast excitatory synaptic transmissions within the mammalian central nervous system (CNS). As for other ion channel protein families, there has been astounding progress in recent years in elucidating the details of protein structure through the crystallization of at least part of the ion channel protein complex. The result is a new framework for the interpretation of both classic and emerging functional data. Here we summarize, compare, and contrast recent findings for the AMPA, kainate, and NMDA subtypes of glutamate receptor ion channels, with an emphasis on the functional and structural aspects of how agonist binding controls channel gating.
authors.affiliation: Department of Pharmacology, Emory University School of Medicine, Rollins Research Center, Atlanta, Georgia 30322-3090, USA. kerrege@emory.edu
authors.forename: Kevin
authors.initials: K
authors.lastname: Erreger
authors.forename: Philip E
authors.initials: PE
authors.lastname: Chen
authors.forename: David J A
authors.initials: DJ
authors.lastname: Wyllie
authors.forename: Stephen F
authors.initials: SF
authors.lastname: Traynelis
mesh_terms: D000818:Animals; D001665:Binding Sites / Q000502:physiology; D002490:Central Nervous System / Q000502:physiology*; D018690:Excitatory Amino Acid Agonists / Q000378:metabolism; D006801:Humans; D015640:Ion Channel Gating / Q000502:physiology*; D007700:Kinetics; D008024:Ligands; D017434:Protein Structure, Tertiary / Q000502:physiology; D017470:Receptors, Glutamate / Q000502:physiology*; D009435:Synaptic Transmission / Q000502:physiology*
chemical_list: D018690:Excitatory Amino Acid Agonists; D008024:Ligands; D017470:Receptors, Glutamate