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Open data
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Basic information
| Entry | Database: PDB / ID: 7lde | ||||||
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| Title | native AMPA receptor | ||||||
Components |
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Keywords | MEMBRANE PROTEIN / neurotransmitter / hippocampus / ion-channel / glycosylation | ||||||
| Function / homology | Function and homology informationnegative regulation of anterograde synaptic vesicle transport / negative regulation of receptor localization to synapse / Phase 0 - rapid depolarisation / Phase 2 - plateau phase / Cargo concentration in the ER / Activation of AMPA receptors / COPII-mediated vesicle transport / Synaptic adhesion-like molecules / Unblocking of NMDA receptors, glutamate binding and activation / Trafficking of GluR2-containing AMPA receptors ...negative regulation of anterograde synaptic vesicle transport / negative regulation of receptor localization to synapse / Phase 0 - rapid depolarisation / Phase 2 - plateau phase / Cargo concentration in the ER / Activation of AMPA receptors / COPII-mediated vesicle transport / Synaptic adhesion-like molecules / Unblocking of NMDA receptors, glutamate binding and activation / Trafficking of GluR2-containing AMPA receptors / cellular response to ammonium ion / axonal spine / LGI-ADAM interactions / positive regulation of locomotion involved in locomotory behavior / positive regulation of membrane potential / localization within membrane / Trafficking of AMPA receptors / response to sucrose / regulation of monoatomic ion transmembrane transport / L-type voltage-gated calcium channel complex / myosin V binding / cellular response to L-glutamate / neuron spine / positive regulation of AMPA receptor activity / proximal dendrite / postsynaptic neurotransmitter receptor diffusion trapping / protein phosphatase 2B binding / response to arsenic-containing substance / regulation of AMPA receptor activity / channel regulator activity / cellular response to dsRNA / long-term synaptic depression / ligand-gated calcium channel activity / dendritic spine membrane / regulation of NMDA receptor activity / beta-2 adrenergic receptor binding / cellular response to peptide hormone stimulus / spinal cord development / response to psychosocial stress / peptide hormone receptor binding / cellular response to amine stimulus / response to morphine / perisynaptic space / neuronal cell body membrane / behavioral response to pain / protein kinase A binding / response to lithium ion / AMPA glutamate receptor activity / regulation of receptor recycling / neuronal action potential / adenylate cyclase binding / transmission of nerve impulse / AMPA glutamate receptor complex / response to electrical stimulus / ionotropic glutamate receptor complex / cellular response to glycine / immunoglobulin binding / asymmetric synapse / G-protein alpha-subunit binding / glutamate receptor binding / regulation of postsynaptic membrane neurotransmitter receptor levels / positive regulation of synaptic transmission / conditioned place preference / long-term memory / postsynaptic density, intracellular component / vesicle-mediated transport / response to fungicide / voltage-gated calcium channel activity / glutamate-gated receptor activity / cellular response to brain-derived neurotrophic factor stimulus / positive regulation of synaptic transmission, glutamatergic / synapse assembly / glutamate-gated calcium ion channel activity / somatodendritic compartment / presynaptic active zone membrane / ionotropic glutamate receptor binding / excitatory synapse / ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / dendrite membrane / positive regulation of excitatory postsynaptic potential / response to cocaine / dendritic shaft / calcium channel regulator activity / synaptic membrane / neuromuscular junction / synaptic transmission, glutamatergic / PDZ domain binding / long-term synaptic potentiation / receptor internalization / transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / cerebral cortex development / regulation of synaptic plasticity / regulation of membrane potential / response to nutrient levels / response to toxic substance / recycling endosome / postsynaptic density membrane / modulation of chemical synaptic transmission / Schaffer collateral - CA1 synapse / small GTPase binding Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.9 Å | ||||||
Authors | Yu, J. / Rao, P. / Gouaux, E. | ||||||
| Funding support | United States, 1items
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Citation | Journal: Nature / Year: 2021Title: Hippocampal AMPA receptor assemblies and mechanism of allosteric inhibition. Authors: Jie Yu / Prashant Rao / Sarah Clark / Jaba Mitra / Taekjip Ha / Eric Gouaux / ![]() Abstract: AMPA-selective glutamate receptors mediate the transduction of signals between the neuronal circuits of the hippocampus. The trafficking, localization, kinetics and pharmacology of AMPA receptors are ...AMPA-selective glutamate receptors mediate the transduction of signals between the neuronal circuits of the hippocampus. The trafficking, localization, kinetics and pharmacology of AMPA receptors are tuned by an ensemble of auxiliary protein subunits, which are integral membrane proteins that associate with the receptor to yield bona fide receptor signalling complexes. Thus far, extensive studies of recombinant AMPA receptor-auxiliary subunit complexes using engineered protein constructs have not been able to faithfully elucidate the molecular architecture of hippocampal AMPA receptor complexes. Here we obtain mouse hippocampal, calcium-impermeable AMPA receptor complexes using immunoaffinity purification and use single-molecule fluorescence and cryo-electron microscopy experiments to elucidate three major AMPA receptor-auxiliary subunit complexes. The GluA1-GluA2, GluA1-GluA2-GluA3 and GluA2-GluA3 receptors are the predominant assemblies, with the auxiliary subunits TARP-γ8 and CNIH2-SynDIG4 non-stochastically positioned at the B'/D' and A'/C' positions, respectively. We further demonstrate how the receptor-TARP-γ8 stoichiometry explains the mechanism of and submaximal inhibition by a clinically relevant, brain-region-specific allosteric inhibitor. | ||||||
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Structure visualization
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| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 7lde.cif.gz | 840.7 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb7lde.ent.gz | 647.3 KB | Display | PDB format |
| PDBx/mmJSON format | 7lde.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ld/7lde ftp://data.pdbj.org/pub/pdb/validation_reports/ld/7lde | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 23284MC ![]() 7lddC ![]() 7lepC M: map data used to model this data C: citing same article ( |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-Protein , 4 types, 8 molecules ACBDEFGH
| #1: Protein | Mass: 101678.969 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #2: Protein | Mass: 98899.883 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #3: Protein | Mass: 18948.420 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #4: Protein | Mass: 43502.938 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Antibody , 3 types, 6 molecules ILJMKN
| #5: Antibody | Mass: 27511.527 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #6: Antibody | Mass: 25111.660 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: Spodoptera aff. frugiperda 1 BOLD-2017 (butterflies/moths)#7: Antibody | Mass: 27975.439 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: Spodoptera aff. frugiperda 1 BOLD-2017 (butterflies/moths) |
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-Sugars , 2 types, 12 molecules 
| #8: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose #14: Sugar | ChemComp-NAG / |
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-Non-polymers , 9 types, 40 molecules 
















| #9: Chemical | ChemComp-ZK1 / {[ #10: Chemical | #11: Chemical | ChemComp-OCT / #12: Chemical | ChemComp-HP6 / #13: Chemical | ChemComp-D10 / #15: Chemical | ChemComp-D12 / #16: Chemical | ChemComp-C14 / #17: Chemical | ChemComp-DD9 / #18: Chemical | |
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-Details
| Has ligand of interest | Y |
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| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
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| Buffer solution | pH: 8 | ||||||||||||||||||||||||||||||
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||||||||
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
| Software | Name: PHENIX / Version: 1.17_3644: / Classification: refinement | ||||||||||||||||||||||||
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 157000 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi






United States, 1items
Citation
UCSF Chimera
















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Spodoptera aff. frugiperda 1 BOLD-2017 (butterflies/moths)
