6NJL

Architecture and subunit arrangement of native AMPA receptors

Summary for 6NJL

• Entry DOI: 10.2210/pdb6njl/pdb
• EMDB information: 9387
• Descriptor: Glutamate receptor 1, 2-acetamido-2-deoxy-beta-D-glucopyranose, Glutamate receptor 2, ... (10 entities in total)
• Functional Keywords: ampa receptor, ligand gated ion channel, neurotransmitter, synapse, membrane protein, membrane protein-immune system complex, membrane protein/immune system
• Biological source: Mus musculus; More
• Total number of polymer chains: 14
• Total formula weight: 665268.70

Authors

Gouaux, E.,Zhao, Y. (deposition date: 2019-01-03, release date: 2019-04-24, Last modification date: 2024-11-06)

Primary citation

Zhao, Y.,Chen, S.,Swensen, A.C.,Qian, W.J.,Gouaux, E.
Architecture and subunit arrangement of native AMPA receptors elucidated by cryo-EM.
Science, 364:355-362, 2019

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 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.

PubMed: 30975770
DOI: 10.1126/science.aaw8250

Experimental method

ELECTRON MICROSCOPY (6.7 Å)