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	Auxiliary subunits reshape structural asymmetry and functional plasticity in heterotetrameric GluA1/A2 AMPA receptor core.
Journal, issue, pages	Nat Commun, Year 2026
Publish date	Mar 28, 2026
Authors	Laura Y Yen / Thomas P Newton / Maria V Yelshanskaya / Muhammed Aktolun / Shanti Pal Gangwar / Rasmus P Clausen / Maria G Kurnikova / Alexander I Sobolevsky /
PubMed Abstract	AMPA-subtype ionotropic glutamate receptors (AMPARs) mediate the fast component of excitatory neurotransmission. They govern synaptic plasticity that underlies learning and memory, while their ...AMPA-subtype ionotropic glutamate receptors (AMPARs) mediate the fast component of excitatory neurotransmission. They govern synaptic plasticity that underlies learning and memory, while their dysregulation is implicated in numerous neurological disorders. The functional diversity of AMPARs arises from variations in their subunit composition and also their association with auxiliary subunits. While multiple structures of homomeric AMPARs have been reported, structural information for the heteromeric core - particularly in the absence of auxiliary subunits, which would serve as a functional and structural baseline - has been limited. Here, we report cryo-electron microscopy structures of GluA1/A2, the most abundant AMPAR di-heteromer in the brain, in the closed, open, and desensitized states. Using molecular dynamics (MD) simulations and cross-correlating structural and functional information, we find that auxiliary subunits increase the diameter of channel pore, which corresponds to larger conductance. Likewise, we find that recovery from desensitization slows with greater disruption of two-fold rotational symmetry of the ligand-binding domain dimer in the desensitized state. Both receptor activation and desensitization vary with the type and number of associated auxiliary proteins. These structures offer a foundation for uncovering how auxiliary subunits reshape structural asymmetry and functional plasticity in heterotetrameric AMPARs.
External links	Nat Commun / PubMed:41904128
Methods	EM (single particle)
Resolution	3.13 - 4.91 Å
Structure data	EMDB-70909: Heteromeric GluA1/A2 in the inactive state, consensus refinement of LBD-TMD Method: EM (single particle) / Resolution: 3.43 Å EMDB-70910: Heteromeric GluA1/A2 in the inactive state, transmembrane domain (TMD) Method: EM (single particle) / Resolution: 3.55 Å EMDB-70911: Heteromeric GluA1/A2 in the inactive state, ligand binding domain (LBD) Method: EM (single particle) / Resolution: 3.51 Å 70912 9ovt EMDB-70912, PDB-9ovt: Heteromeric GluA1/A2 in the inactive state, composite map of LBD-TMD Method: EM (single particle) / Resolution: 3.43 Å EMDB-70913: Heteromeric GluA1/A2 in the activated state, consensus refinement of ATD-LBD-TMD Method: EM (single particle) / Resolution: 3.3 Å EMDB-70914: Heteromeric GluA1/A2 in the activated state, ligand binding domain (LBD) Method: EM (single particle) / Resolution: 3.13 Å EMDB-70915: Heteromeric GluA1/A2 in the activated state, transmembrane domain (TMD) Method: EM (single particle) / Resolution: 3.81 Å EMDB-70916: Heteromeric GluA1/A2-CNIH1 in the activated state, consensus refinement of LBD-TMD Method: EM (single particle) / Resolution: 3.76 Å EMDB-70917: Heteromeric GluA1/A2-CNIH1 in the activated state, ligand binding domain (LBD) Method: EM (single particle) / Resolution: 3.51 Å EMDB-70918: Heteromeric GluA1/A2-CNIH1 in the activated state, transmembrane domain (TMD) Method: EM (single particle) / Resolution: 3.55 Å 70919 9ovu EMDB-70919, PDB-9ovu: Composite map of GluA1/A2 in the activated state, in complex with positive allosteric modulator (R,R)-2b and agonist glutamate (ATD-LBD-TMD) Method: EM (single particle) / Resolution: 3.2 Å 70920 9ovv EMDB-70920, PDB-9ovv: Heteromeric GluA1/A2-CNIH1 in the activated state, composite map of LBD-TMD Method: EM (single particle) / Resolution: 3.76 Å EMDB-70921: Heteromeric GluA1/A2 in the desensitized state, consensus refinement of ATD-LBD-TMD Method: EM (single particle) / Resolution: 4.91 Å EMDB-70922: Heteromeric GluA1/A2 in the desensitized state, amino-terminal domain (ATD) Method: EM (single particle) / Resolution: 4.28 Å EMDB-70923: Heteromeric GluA1/A2 in the desensitized state, ligand binding domain (LBD) Method: EM (single particle) / Resolution: 4.59 Å EMDB-70924: Heteromeric GluA1/A2 in the desensitized state, transmembrane domain (TMD) Method: EM (single particle) / Resolution: 4.57 Å 70925 9ovw EMDB-70925, PDB-9ovw: Heteromeric GluA1/A2 in the desensitized state, composite map of ATD-LBD-TMD Method: EM (single particle) / Resolution: 4.91 Å EMDB-75274: Heteromeric GluA1/A2 in the activated state, amino-terminal domain (ATD) Method: EM (single particle) / Resolution: 3.94 Å
Chemicals	ChemComp-ZK1: {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid / antagonist, medicationYM ChemComp-NA: Unknown entry ChemComp-HOH: WATER ChemComp-GLU: GLUTAMIC ACID ChemComp-FWF: N,N'-[biphenyl-4,4'-diyldi(2R)propane-2,1-diyl]dipropane-2-sulfonamide ChemComp-POV: (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate / phospholipidYM ChemComp-QUS: (S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC ACID / agonist*YM
Source	rattus norvegicus (Norway rat) homo sapiens (human)
Keywords	MEMBRANE PROTEIN / GluA1A2 heterotetramer ZK iGluR / GluA1A2 heterotetramer active iGluR / GluA1A2-CNIH2 heterotetramer active iGluR / GluA1A2 heterotetramer quisqualate iGluR