11VV
GluA2-STZ apo state (full-length composite)
Summary for 11VV
| Entry DOI | 10.2210/pdb11vv/pdb |
| EMDB information | 76084 |
| Descriptor | Isoform Flip of Glutamate receptor 2,Voltage-dependent calcium channel gamma-2 subunit, (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate, SODIUM ION (3 entities in total) |
| Functional Keywords | ionotropic glutamate receptor (iglur), iglur, glua2, transmembrane ampar regulatory protein (tarp) y2, gamma2, stargazin (stz), membrane protein |
| Biological source | Rattus norvegicus (Norway rat) More |
| Total number of polymer chains | 4 |
| Total formula weight | 483712.06 |
| Authors | Gangwar, S.P.,Newton, T.P.,Yen, L.Y.,Sobolevsky, A.I. (deposition date: 2026-03-15, release date: 2026-09-23) |
| Primary citation | Newton, T.P.,Aktolun, M.,Yelshanskaya, M.V.,Alekseev, A.A.,Yen, L.Y.,Gangwar, S.P.,Sobolevsky, I.A.,Kurnikova, M.G.,Sobolevsky, A.I. Pre-activation and gating pathway of AMPA receptors revealed by full and partial agonists. Nat.Struct.Mol.Biol., 2026 Cited by PubMed Abstract: AMPA receptors (AMPARs) mediate fast excitatory neurotransmission. Gating of AMPARs starts with agonist binding and transition into a non-conducting pre-active state, followed by transition into conducting open or non-conducting desensitized states. While the terminal apo, open and desensitized states have been structurally characterized, the intermediate pre-active state has remained an enigma. Compared to full agonist glutamate, partial agonists reduce the maximal occupancy of the open state and increase the probability of the pre-active state occurrence. Here we use different partial agonists and time-resolved cryo-electron microscopy (cryo-EM) to capture a structural ensemble of GluA2-γ2 AMPAR complexes in the closed apo, pre-active, open and desensitized states. Binding of partial agonists to the ligand-binding domain (LBD) results in different extents of LBD clamshell closure, with closures exceeding a threshold of ~17° resulting in the open and desensitized states and smaller closures stabilizing the pre-active state. The pre-active state has a distinct gate conformation intermediate between the other two discrete states, completely open and closed. Combined with single-channel current recordings and molecular dynamics simulations, our structural results reveal the complete gating pathway of AMPARs and shed light on the molecular mechanisms of partial agonism and pre-activation. PubMed: 42717062DOI: 10.1038/s41594-026-01882-9 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.93 Å) |
Structure validation
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