6UCB

GluA2 in complex with its auxiliary subunit CNIH3 - with antagonist ZK200775, LBD, TMD, CNIH3, and lipids

Summary for 6UCB

• Entry DOI: 10.2210/pdb6ucb/pdb
• EMDB information: 20330 20654 20666 20727
• Descriptor: Glutamate receptor 2, Protein cornichon homolog 3, {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid, ... (6 entities in total)
• Functional Keywords: ionotropic glutamate receptor, ampa receptor, cornichon, auxiliary subunit, ion channel, ligand gated ion channel, synaptic transmission, excitatory synaptic transmission, neurotransmitter receptor, stargazin, tarp, zk200775, lipid, mpqx, transport protein
• Biological source: Rattus norvegicus (Rat); More
• Total number of polymer chains: 8
• Total formula weight: 488770.26

Authors

Nakagawa, T. (deposition date: 2019-09-15, release date: 2019-12-04, Last modification date: 2024-11-13)

Primary citation

Nakagawa, T.
Structures of the AMPA receptor in complex with its auxiliary subunit cornichon.
Science, 366:1259-1263, 2019

PubMed Abstract: In the brain, AMPA-type glutamate receptors (AMPARs) form complexes with their auxiliary subunits and mediate the majority of fast excitatory neurotransmission. Signals transduced by these complexes are critical for synaptic plasticity, learning, and memory. The two major categories of AMPAR auxiliary subunits are transmembrane AMPAR regulatory proteins (TARPs) and cornichon homologs (CNIHs); these subunits share little homology and play distinct roles in controlling ion channel gating and trafficking of AMPAR. Here, I report high-resolution cryo-electron microscopy structures of AMPAR in complex with CNIH3. Contrary to its predicted membrane topology, CNIH3 lacks an extracellular domain and instead contains four membrane-spanning helices. The protein-protein interaction interface that dictates channel modulation and the lipids surrounding the complex are revealed. These structures provide insights into the molecular mechanism for ion channel modulation and assembly of AMPAR/CNIH3 complexes.

PubMed: 31806817
DOI: 10.1126/science.aay2783

Experimental method

ELECTRON MICROSCOPY (3.28 Å)