5IDF
Cryo-EM structure of GluA2/3 AMPA receptor heterotetramer (model II)
Summary for 5IDF
| Entry DOI | 10.2210/pdb5idf/pdb |
| Related | 5fwy |
| EMDB information | 8091 |
| Descriptor | Glutamate receptor 2, Glutamate receptor 3 (2 entities in total) |
| Functional Keywords | ampa glutamate receptor, signaling protein |
| Biological source | Rattus norvegicus (Norway rat) More |
| Cellular location | Cell membrane; Multi-pass membrane protein: P19491 P19492 |
| Total number of polymer chains | 4 |
| Total formula weight | 393477.70 |
| Authors | Herguedas, B.,Garcia-Nafria, J.,Fernandez-Leiro, R.,Greger, I.H. (deposition date: 2016-02-24, release date: 2016-03-16, Last modification date: 2024-05-15) |
| Primary citation | Herguedas, B.,Garcia-Nafria, J.,Cais, O.,Fernandez-Leiro, R.,Krieger, J.,Ho, H.,Greger, I.H. Structure and organization of heteromeric AMPA-type glutamate receptors. Science, 352:aad3873-aad3873, 2016 Cited by PubMed Abstract: AMPA-type glutamate receptors (AMPARs), which are central mediators of rapid neurotransmission and synaptic plasticity, predominantly exist as heteromers of the subunits GluA1 to GluA4. Here we report the first AMPAR heteromer structures, which deviate substantially from existing GluA2 homomer structures. Crystal structures of the GluA2/3 and GluA2/4 N-terminal domains reveal a novel compact conformation with an alternating arrangement of the four subunits around a central axis. This organization is confirmed by cysteine cross-linking in full-length receptors, and it permitted us to determine the structure of an intact GluA2/3 receptor by cryogenic electron microscopy. Two models in the ligand-free state, at resolutions of 8.25 and 10.3 angstroms, exhibit substantial vertical compression and close associations between domain layers, reminiscent of N-methyl-D-aspartate receptors. Model 1 resembles a resting state and model 2 a desensitized state, thus providing snapshots of gating transitions in the nominal absence of ligand. Our data reveal organizational features of heteromeric AMPARs and provide a framework to decipher AMPAR architecture and signaling. PubMed: 26966189DOI: 10.1126/science.aad3873 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (10.31 Å) |
Structure validation
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