Click here to close
Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly.
We suggest using a current version of Chrome,
FireFox, or Safari.
Structure
2011 Oct 12;1910:1370-80. doi: 10.1016/j.str.2011.08.009.
Show Gene links
Show Anatomy links
Emerging models of glutamate receptor ion channel structure and function.
Mayer ML.
???displayArticle.abstract???
Excitatory synaptic transmission in the brain is mediated by ligand-gated ion channels (iGluRs) activated by glutamate. Distinct from other neurotransmitter receptors, the extracellular domains of iGluRs are loosely packed assemblies with two clearly distinct layers, each of which has both local and global 2-fold axes of symmetry. By contrast, the iGluR transmembrane segments have 4-fold symmetry and share a conserved pore loop architecture found in tetrameric voltage-gated ion channels. The striking layered architecture of iGluRs revealed by the 3.6 Å resolution structure of an AMPA receptor homotetramer likely arose from gene fusion events that occurred early in evolution. Although this modular design has greatly facilitated biophysical and structural studies on individual iGluR domains, and suggested conserved mechanisms for iGluR gating, recent work is beginning to reveal unanticipated diversity in the structure, allosteric regulation, and assembly of iGluR subtypes.
Abuin,
Functional architecture of olfactory ionotropic glutamate receptors.
2011, Pubmed
Abuin,
Functional architecture of olfactory ionotropic glutamate receptors.
2011,
Pubmed Armstrong,
Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core.
2000,
Pubmed Armstrong,
Tuning activation of the AMPA-sensitive GluR2 ion channel by genetic adjustment of agonist-induced conformational changes.
2003,
Pubmed
,
Xenbase Ayalon,
Two regions in the N-terminal domain of ionotropic glutamate receptor 3 form the subunit oligomerization interfaces that control subtype-specific receptor assembly.
2005,
Pubmed Benton,
Variant ionotropic glutamate receptors as chemosensory receptors in Drosophila.
2009,
Pubmed Chaudhry,
Stability of ligand-binding domain dimer assembly controls kainate receptor desensitization.
2009,
Pubmed Clayton,
Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors.
2009,
Pubmed Das,
Domain organization and function in GluK2 subtype kainate receptors.
2010,
Pubmed Farina,
Separation of domain contacts is required for heterotetrameric assembly of functional NMDA receptors.
2011,
Pubmed Fenwick,
NMR spectroscopy of the ligand-binding core of ionotropic glutamate receptor 2 bound to 5-substituted willardiine partial agonists.
2008,
Pubmed Furukawa,
Subunit arrangement and function in NMDA receptors.
2005,
Pubmed Gielen,
Structural rearrangements of NR1/NR2A NMDA receptors during allosteric inhibition.
2008,
Pubmed
,
Xenbase Gielen,
Mechanism of differential control of NMDA receptor activity by NR2 subunits.
2009,
Pubmed He Xl,
Allosteric activation of a spring-loaded natriuretic peptide receptor dimer by hormone.
2001,
Pubmed Horning,
Regulation of AMPA receptor gating by ligand binding core dimers.
2004,
Pubmed Jackson,
The expanding social network of ionotropic glutamate receptors: TARPs and other transmembrane auxiliary subunits.
2011,
Pubmed Jin,
Crystal structure and association behaviour of the GluR2 amino-terminal domain.
2009,
Pubmed Jin,
Structural basis for partial agonist action at ionotropic glutamate receptors.
2003,
Pubmed
,
Xenbase Karakas,
Structure of the zinc-bound amino-terminal domain of the NMDA receptor NR2B subunit.
2009,
Pubmed
,
Xenbase Karakas,
Subunit arrangement and phenylethanolamine binding in GluN1/GluN2B NMDA receptors.
2011,
Pubmed
,
Xenbase Kumar,
Crystal structures of the glutamate receptor ion channel GluK3 and GluK5 amino-terminal domains.
2010,
Pubmed Kumar,
Structure and assembly mechanism for heteromeric kainate receptors.
2011,
Pubmed
,
Xenbase Kumar,
The N-terminal domain of GluR6-subtype glutamate receptor ion channels.
2009,
Pubmed Landes,
Structural landscape of isolated agonist-binding domains from single AMPA receptors.
2011,
Pubmed Lau,
The hidden energetics of ligand binding and activation in a glutamate receptor.
2011,
Pubmed Lau,
The free energy landscapes governing conformational changes in a glutamate receptor ligand-binding domain.
2007,
Pubmed Lee,
Amino terminal domains of the NMDA receptor are organized as local heterodimers.
2011,
Pubmed Maltsev,
Mechanism of partial agonism at the GluR2 AMPA receptor: Measurements of lobe orientation in solution.
2008,
Pubmed Mayer,
Glutamate receptors at atomic resolution.
2006,
Pubmed Mayer,
Structure and function of glutamate receptor ion channels.
2004,
Pubmed Nakagawa,
Structure and different conformational states of native AMPA receptor complexes.
2005,
Pubmed Nayeem,
A nondesensitizing kainate receptor point mutant.
2009,
Pubmed Pasternack,
Alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor channels lacking the N-terminal domain.
2002,
Pubmed Plested,
AMPA receptor ligand binding domain mobility revealed by functional cross linking.
2009,
Pubmed Plested,
Structure and mechanism of kainate receptor modulation by anions.
2007,
Pubmed Pøhlsgaard,
Lessons from more than 80 structures of the GluA2 ligand-binding domain in complex with agonists, antagonists and allosteric modulators.
2011,
Pubmed Poon,
Mechanisms of modal activation of GluA3 receptors.
2011,
Pubmed Qiu,
An endoplasmic reticulum retention signal located in the extracellular amino-terminal domain of the NR2A subunit of N-Methyl-D-aspartate receptors.
2009,
Pubmed Rachline,
The micromolar zinc-binding domain on the NMDA receptor subunit NR2B.
2005,
Pubmed
,
Xenbase Robert,
AMPA receptor binding cleft mutations that alter affinity, efficacy, and recovery from desensitization.
2005,
Pubmed Rossmann,
Subunit-selective N-terminal domain associations organize the formation of AMPA receptor heteromers.
2011,
Pubmed Salussolia,
Arrangement of subunits in functional NMDA receptors.
2011,
Pubmed
,
Xenbase Sobolevsky,
X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor.
2009,
Pubmed Stawski,
Pharmacology of ionotropic glutamate receptors: A structural perspective.
2010,
Pubmed Straub,
Distinct functions of kainate receptors in the brain are determined by the auxiliary subunit Neto1.
2011,
Pubmed Stroebel,
Functional evidence for a twisted conformation of the NMDA receptor GluN2A subunit N-terminal domain.
2011,
Pubmed Sukumaran,
Dynamics and allosteric potential of the AMPA receptor N-terminal domain.
2011,
Pubmed Sun,
Mechanism of glutamate receptor desensitization.
2002,
Pubmed Traynelis,
Glutamate receptor ion channels: structure, regulation, and function.
2010,
Pubmed Watkins,
The glutamate story.
2006,
Pubmed Weston,
Conformational restriction blocks glutamate receptor desensitization.
2006,
Pubmed Weston,
Interdomain interactions in AMPA and kainate receptors regulate affinity for glutamate.
2006,
Pubmed Wilding,
Fatty acid modulation and polyamine block of GluK2 kainate receptors analyzed by scanning mutagenesis.
2010,
Pubmed Yao,
Crystal structure of the glutamate receptor GluA1 N-terminal domain.
2011,
Pubmed Yuan,
Control of NMDA receptor function by the NR2 subunit amino-terminal domain.
2009,
Pubmed
,
Xenbase Zhang,
Structural and single-channel results indicate that the rates of ligand binding domain closing and opening directly impact AMPA receptor gating.
2008,
Pubmed
