6UD4

GluA2 in complex with its auxiliary subunit CNIH3 in AS map II - (LBD-TMD-C3(AS) II)- with antagonist ZK200775, without NTD

6UD4 の概要

• エントリーDOI: 10.2210/pdb6ud4/pdb
• EMDBエントリー: 20330 20332 20654 20666 20717 20727 20732 20733
• 分子名称: 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, ... (5 entities in total)
• 機能のキーワード: ionotropic glutamate receptor, ampa receptor, cornichon, auxiliary subunit, ion channel, ligand gated ion channel, synaptic transmission, excitatory synaptic transmission, neurotransmitter receptor, stargazin, tarp, lipid, mpqx, transport protein
• 由来する生物種: Rattus norvegicus (Rat); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 483782.39

構造登録者

Nakagawa, T. (登録日: 2019-09-18, 公開日: 2019-12-04, 最終更新日: 2024-10-16)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (3.3 Å)