Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural mobility tunes signalling of the GluA1 AMPA glutamate receptor.
Journal, issue, pages	Nature, Vol. 621, Issue 7980, Page 877-882, Year 2023
Publish date	Sep 13, 2023
Authors	Danyang Zhang / Josip Ivica / James M Krieger / Hinze Ho / Keitaro Yamashita / Imogen Stockwell / Rozbeh Baradaran / Ondrej Cais / Ingo H Greger /
PubMed Abstract	AMPA glutamate receptors (AMPARs), the primary mediators of excitatory neurotransmission in the brain, are either GluA2 subunit-containing and thus Ca-impermeable, or GluA2-lacking and Ca-permeable. ...AMPA glutamate receptors (AMPARs), the primary mediators of excitatory neurotransmission in the brain, are either GluA2 subunit-containing and thus Ca-impermeable, or GluA2-lacking and Ca-permeable. Despite their prominent expression throughout interneurons and glia, their role in long-term potentiation and their involvement in a range of neuropathologies, structural information for GluA2-lacking receptors is currently absent. Here we determine and characterize cryo-electron microscopy structures of the GluA1 homotetramer, fully occupied with TARPγ3 auxiliary subunits (GluA1/γ3). The gating core of both resting and open-state GluA1/γ3 closely resembles GluA2-containing receptors. However, the sequence-diverse N-terminal domains (NTDs) give rise to a highly mobile assembly, enabling domain swapping and subunit re-alignments in the ligand-binding domain tier that are pronounced in desensitized states. These transitions underlie the unique kinetic properties of GluA1. A GluA2 mutant (F231A) increasing NTD dynamics phenocopies this behaviour, and exhibits reduced synaptic responses, reflecting the anchoring function of the AMPAR NTD at the synapse. Together, this work underscores how the subunit-diverse NTDs determine subunit arrangement, gating properties and ultimately synaptic signalling efficiency among AMPAR subtypes.
External links	Nature / PubMed:37704721 / PubMed Central
Methods	EM (single particle)
Resolution	2.64 - 3.77 Å
Structure data	16379 8c1p EMDB-16379, PDB-8c1p: Active state homomeric GluA1 AMPA receptor in complex with TARP gamma 3 Method: EM (single particle) / Resolution: 2.9 Å 16380 8c1q EMDB-16380, PDB-8c1q: Resting state homomeric GluA1 AMPA receptor in complex with TARP gamma 3 Method: EM (single particle) / Resolution: 2.82 Å 16381 8c1r EMDB-16381, PDB-8c1r: Resting state homomeric GluA2 F231A mutant AMPA receptor in complex with TARP gamma-2 Method: EM (single particle) / Resolution: 3.2 Å 16382 8c1s EMDB-16382, PDB-8c1s: Transmembrane domain of resting state homomeric GluA2 F231A mutant AMPA receptor in complex with TARP gamma 2 Method: EM (single particle) / Resolution: 3.0 Å 16390 8c2h EMDB-16390, PDB-8c2h: Transmembrane domain of active state homomeric GluA1 AMPA receptor in tandem with TARP gamma 3 Method: EM (single particle) / Resolution: 2.64 Å 16391 8c2i EMDB-16391, PDB-8c2i: Transmembrane domain of resting state homomeric GluA1 AMPA receptor in complex with TARP gamma 3 Method: EM (single particle) / Resolution: 2.7 Å 17392 8p3q EMDB-17392, PDB-8p3q: Homomeric GluA2 flip R/G-unedited Q/R-edited F231A mutant in tandem with TARP gamma-2, desensitized conformation 3 Method: EM (single particle) / Resolution: 2.95 Å 17393 8p3s EMDB-17393, PDB-8p3s: Homomeric GluA2 flip R/G-unedited Q/R-edited F231A mutant in tandem with TARP gamma-2, desensitized conformation 2 Method: EM (single particle) / Resolution: 2.95 Å 17394 8p3t EMDB-17394, PDB-8p3t: Homomeric GluA1 in tandem with TARP gamma-3, desensitized conformation 1 Method: EM (single particle) / Resolution: 3.39 Å 17395 8p3u EMDB-17395, PDB-8p3u: Homomeric GluA1 in tandem with TARP gamma-3, desensitized conformation 2 Method: EM (single particle) / Resolution: 3.77 Å 17396 8p3v EMDB-17396, PDB-8p3v: Homomeric GluA1 in tandem with TARP gamma-3, desensitized conformation 3 Method: EM (single particle) / Resolution: 3.53 Å 17397 8p3w EMDB-17397, PDB-8p3w: Homomeric GluA1 in tandem with TARP gamma-3, desensitized conformation 4 Method: EM (single particle) / Resolution: 3.53 Å 17398 8p3x EMDB-17398, PDB-8p3x: Homomeric GluA2 flip R/G-edited Q/R-edited F231A mutant in tandem with TARP gamma-2, desensitized conformation 1 Method: EM (single particle) / Resolution: 3.36 Å 17399 8p3y EMDB-17399, PDB-8p3y: Homomeric GluA2 flip R/G-edited Q/R-edited F231A mutant in tandem with TARP gamma-2, desensitized conformation 3 Method: EM (single particle) / Resolution: 3.55 Å 17400 8p3z EMDB-17400, PDB-8p3z: Homomeric GluA2 flip R/G-edited Q/R-edited F231A mutant in tandem with TARP gamma-2, desensitized conformation 2 Method: EM (single particle) / Resolution: 3.46 Å 17692 8piv EMDB-17692, PDB-8piv: Homomeric GluA2 flip R/G-unedited Q/R-edited F231A mutant in tandem with TARP gamma-2, desensitized conformation 1 Method: EM (single particle) / Resolution: 3.46 Å
Chemicals	ChemComp-CYZ: CYCLOTHIAZIDE ChemComp-PLM: PALMITIC ACID ChemComp-OLC: (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate ChemComp-GLU: GLUTAMIC ACID ChemComp-POV: (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate / phospholipidYM ChemComp-HOH: WATER ChemComp-ZK1: {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid / antagonist, medicationYM
Source	Rattus (rat) rattus norvegicus (Norway rat)
Keywords	MEMBRANE PROTEIN / AMPAR / ion channels / neurotransmission / AMPA-type glutamate neurotransmitter receptor / auxiliary subunit complex / agonist / desensitized