5WEN
GluA2 bound to GSG1L in digitonin, state 2
Summary for 5WEN
| Entry DOI | 10.2210/pdb5wen/pdb |
| EMDB information | 8819 8820 8821 8822 8823 |
| Descriptor | Glutamate receptor 2,Germ cell-specific gene 1-like protein, Digitonin (2 entities in total) |
| Functional Keywords | ion channel, transport protein |
| Biological source | Rattus norvegicus (Rat) More |
| Total number of polymer chains | 4 |
| Total formula weight | 472343.47 |
| Authors | Twomey, E.C.,Yelshanskaya, M.V.,Grassucci, R.A.,Frank, J.,Sobolevsky, A.I. (deposition date: 2017-07-10, release date: 2017-08-02, Last modification date: 2025-05-21) |
| Primary citation | Twomey, E.C.,Yelshanskaya, M.V.,Grassucci, R.A.,Frank, J.,Sobolevsky, A.I. Channel opening and gating mechanism in AMPA-subtype glutamate receptors. Nature, 549:60-65, 2017 Cited by PubMed Abstract: AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid)-subtype ionotropic glutamate receptors mediate fast excitatory neurotransmission throughout the central nervous system. Gated by the neurotransmitter glutamate, AMPA receptors are critical for synaptic strength, and dysregulation of AMPA receptor-mediated signalling is linked to numerous neurological diseases. Here we use cryo-electron microscopy to solve the structures of AMPA receptor-auxiliary subunit complexes in the apo, antagonist- and agonist-bound states and determine the iris-like mechanism of ion channel opening. The ion channel selectivity filter is formed by the extended portions of the re-entrant M2 loops, while the helical portions of M2 contribute to extensive hydrophobic interfaces between AMPA receptor subunits in the ion channel. We show how the permeation pathway changes upon channel opening and identify conformational changes throughout the entire AMPA receptor that accompany activation and desensitization. Our findings provide a framework for understanding gating across the family of ionotropic glutamate receptors and the role of AMPA receptors in excitatory neurotransmission. PubMed: 28737760DOI: 10.1038/nature23479 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (6.8 Å) |
Structure validation
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