6FQH
GluA2(flop) S729C ligand binding core dimer bound to NBQX at 1.76 Angstrom resolution
Summary for 6FQH
| Entry DOI | 10.2210/pdb6fqh/pdb |
| Descriptor | Glutamate receptor 2,Glutamate receptor 2, 6-nitro-2,3-bis(oxidanylidene)-1,4-dihydrobenzo[f]quinoxaline-7-sulfonamide (3 entities in total) |
| Functional Keywords | ampar receptor, ligand binding core, competitive antagonist, membrane protein |
| Biological source | Rattus norvegicus (Norway Rat) More |
| Total number of polymer chains | 2 |
| Total formula weight | 61506.47 |
| Authors | Coombs, I.D.,Soto, D.,Gold, M.G.,Farrant, M.F.,Cull-Candy, S.G. (deposition date: 2018-02-14, release date: 2019-03-13, Last modification date: 2024-11-06) |
| Primary citation | Coombs, I.D.,Soto, D.,McGee, T.P.,Gold, M.G.,Farrant, M.,Cull-Candy, S.G. Homomeric GluA2(R) AMPA receptors can conduct when desensitized. Nat Commun, 10:4312-4312, 2019 Cited by PubMed Abstract: Desensitization is a canonical property of ligand-gated ion channels, causing progressive current decline in the continued presence of agonist. AMPA-type glutamate receptors (AMPARs), which mediate fast excitatory signaling throughout the brain, exhibit profound desensitization. Recent cryo-EM studies of AMPAR assemblies show their ion channels to be closed in the desensitized state. Here we present evidence that homomeric Q/R-edited AMPARs still allow ions to flow when the receptors are desensitized. GluA2(R) expressed alone, or with auxiliary subunits (γ-2, γ-8 or GSG1L), generates large fractional steady-state currents and anomalous current-variance relationships. Our results from fluctuation analysis, single-channel recording, and kinetic modeling, suggest that the steady-state current is mediated predominantly by conducting desensitized receptors. When combined with crystallography this unique functional readout of a hitherto silent state enabled us to examine cross-linked cysteine mutants to probe the conformation of the desensitized ligand binding domain of functioning AMPAR complexes. PubMed: 31541113DOI: 10.1038/s41467-019-12280-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75940018229 Å) |
Structure validation
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