|Title||Architecture and subunit arrangement of native AMPA receptors elucidated by cryo-EM.|
|Journal, issue, pages||Science, Vol. 364, Issue 6438, Page 355-362, Year 2019|
|Publish date||Apr 26, 2019|
|Authors||Yan Zhao / Shanshuang Chen / Adam C Swensen / Wei-Jun Qian / Eric Gouaux /|
|PubMed Abstract||Glutamate-gated AMPA receptors mediate the fast component of excitatory signal transduction at chemical synapses throughout all regions of the mammalian brain. AMPA receptors are tetrameric ...Glutamate-gated AMPA receptors mediate the fast component of excitatory signal transduction at chemical synapses throughout all regions of the mammalian brain. AMPA receptors are tetrameric assemblies composed of four subunits, GluA1-GluA4. Despite decades of study, the subunit composition, subunit arrangement, and molecular structure of native AMPA receptors remain unknown. Here we elucidate the structures of 10 distinct native AMPA receptor complexes by single-particle cryo-electron microscopy (cryo-EM). We find that receptor subunits are arranged nonstochastically, with the GluA2 subunit preferentially occupying the B and D positions of the tetramer and with triheteromeric assemblies comprising a major population of native AMPA receptors. Cryo-EM maps define the structure for S2-M4 linkers between the ligand-binding and transmembrane domains, suggesting how neurotransmitter binding is coupled to ion channel gating.|
|External links||Science / PubMed:30975770 / PubMed Central|
|Methods||EM (single particle)|
|Resolution||4.5 - 32 Å|
|Keywords||Animals / Brain / Cryoelectron Microscopy / Ion Channel Gating / Protein Conformation / Protein Multimerization / Protein Subunits / Rats / Receptors, AMPA / Single Molecule Imaging / MEMBRANE PROTEIN/IMMUNE SYSTEM / AMPA receptor / ligand gated ion channel / neurotransmitter / synapse / MEMBRANE PROTEIN / MEMBRANE PROTEIN-IMMUNE SYSTEM complex|
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