|Entry||Database: PDB / ID: 5vhz|
|Title||GluA2-2xGSG1L bound to L-Quisqualate|
|Components||Glutamate receptor 2,Germ cell-specific gene 1-like protein|
|Keywords||TRANSPORT PROTEIN / Ion channel|
|Function / homology||Ionotropic glutamate receptor, metazoa / Periplasmic binding protein-like I / Receptor, ligand binding region / GSG1-like / Ionotropic glutamate receptor, L-glutamate and glycine-binding domain / Ligated ion channel L-glutamate- and glycine-binding site / GSG1-like protein / Receptor family ligand binding region / Ligand-gated ion channel / Ionotropic glutamate receptor ...Ionotropic glutamate receptor, metazoa / Periplasmic binding protein-like I / Receptor, ligand binding region / GSG1-like / Ionotropic glutamate receptor, L-glutamate and glycine-binding domain / Ligated ion channel L-glutamate- and glycine-binding site / GSG1-like protein / Receptor family ligand binding region / Ligand-gated ion channel / Ionotropic glutamate receptor / regulation of AMPA receptor activity / regulation of postsynaptic neurotransmitter receptor activity / AMPA glutamate receptor activity / asymmetric synapse / AMPA glutamate receptor complex / kainate selective glutamate receptor activity / ionotropic glutamate receptor complex / response to lithium ion / regulation of receptor recycling / SNARE binding / positive regulation of synaptic transmission / transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential / integral component of postsynaptic membrane / regulation of synaptic transmission, glutamatergic / response to fungicide / integral component of postsynaptic density membrane / ionotropic glutamate receptor activity / ionotropic glutamate receptor signaling pathway / cytoskeletal protein binding / synaptic vesicle membrane / dendritic shaft / dendrite cytoplasm / receptor internalization / integral component of presynaptic membrane / PDZ domain binding / Schaffer collateral - CA1 synapse / presynaptic membrane / terminal bouton / establishment of protein localization / protein tetramerization / growth cone / chemical synaptic transmission / amyloid-beta binding / ATPase binding / perikaryon / signaling receptor activity / dendritic spine / postsynaptic density / cell junction / synapse / glutamatergic synapse / dendrite / endoplasmic reticulum membrane / neuronal cell body / protein kinase binding / integral component of plasma membrane / cell surface / protein-containing complex / identical protein binding / plasma membrane / Germ cell-specific gene 1-like protein / Glutamate receptor 2|
Function and homology information
|Specimen source||Rattus norvegicus (Norway rat)|
|Method||ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / 8.4 Å resolution|
|Authors||Twomey, E.C. / Yelshanskaya, M.V. / Grassucci, R.A. / Frank, J. / Sobolevsky, A.I.|
|Citation||Journal: Neuron / Year: 2017|
Title: Structural Bases of Desensitization in AMPA Receptor-Auxiliary Subunit Complexes.
Authors: Edward C Twomey / Maria V Yelshanskaya / Robert A Grassucci / Joachim Frank / Alexander I Sobolevsky
Abstract: Fast excitatory neurotransmission is mediated by AMPA-subtype ionotropic glutamate receptors (AMPARs). AMPARs, localized at post-synaptic densities, are regulated by transmembrane auxiliary subunits ...Fast excitatory neurotransmission is mediated by AMPA-subtype ionotropic glutamate receptors (AMPARs). AMPARs, localized at post-synaptic densities, are regulated by transmembrane auxiliary subunits that modulate AMPAR assembly, trafficking, gating, and pharmacology. Aberrancies in AMPAR-mediated signaling are associated with numerous neurological disorders. Here, we report cryo-EM structures of an AMPAR in complex with the auxiliary subunit GSG1L in the closed and desensitized states. GSG1L favors the AMPAR desensitized state, where channel closure is facilitated by profound structural rearrangements in the AMPAR extracellular domain, with ligand-binding domain dimers losing their local 2-fold rotational symmetry. Our structural and functional experiments suggest that AMPAR auxiliary subunits share a modular architecture and use a common transmembrane scaffold for distinct extracellular modules to differentially regulate AMPAR gating. By comparing the AMPAR-GSG1L complex structures, we map conformational changes accompanying AMPAR recovery from desensitization and reveal structural bases for regulation of synaptic transmission by auxiliary subunits.
SummaryFull reportAbout validation report
|Date||Deposition: Apr 13, 2017 / Release: May 3, 2017|
|Structure viewer||Molecule: |
Downloads & links
A: Glutamate receptor 2,Germ cell-specific gene 1-like protein
B: Glutamate receptor 2,Germ cell-specific gene 1-like protein
C: Glutamate receptor 2,Germ cell-specific gene 1-like protein
D: Glutamate receptor 2,Germ cell-specific gene 1-like protein
E: Glutamate receptor 2,Germ cell-specific gene 1-like protein
F: Glutamate receptor 2,Germ cell-specific gene 1-like protein
Mass: 117471.211 Da / Num. of mol.: 6 / Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Gria2, Glur2, Gsg1l / Cell line (production host): HEK-293S / Production host: Homo sapiens (human) / References: UniProt: P19491, UniProt: D3ZK93
ChemComp-QUS / (
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: PARTICLE / Reconstruction method: single particle reconstruction|
|Component||Name: GluA2-2xGSG1L bound to L-Quisqualate cryo-EM density / Type: COMPLEX / Entity ID: 1,||Molecular weight||Experimental value: NO||Source (natural)||Organism: Rattus norvegicus (Norway rat)||Source (recombinant)||Organism: Rattus norvegicus (Norway rat)||Buffer solution||pH: 8||Specimen||Conc.: 5 mg/ml / Details: GluA2-2xGSG1L bound to L-Quisqualate / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES||Specimen support||Details: Gold-gold grids, hydrogen and oxygen glow discharge (20s, 10 watts, 6.4 sccm H2, 27.5 sccm O2)|
Grid material: GOLD / Grid mesh size: 200 / Grid type: C-flat-1.2/1.3
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 295 kelvins|
-Electron microscopy imaging
Model: Tecnai Polara / Image courtesy: FEI Company
|Microscopy||Microscope model: FEI POLARA 300|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: SPOT SCAN|
|Electron lens||Mode: BRIGHT FIELDBright-field microscopy|
|Image recording||Electron dose: 67 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k)|
|CTF correction||Type: PHASE FLIPPING AND AMPLITUDE CORRECTION|
|Symmetry||Point symmetry: C2|
|3D reconstruction||Resolution: 8.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number of particles: 51130 / Symmetry type: POINT|
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