5KBS

Cryo-EM structure of GluA2-0xSTZ at 8.7 Angstrom resolution

5KBS の概要

• エントリーDOI: 10.2210/pdb5kbs/pdb
• 関連するPDBエントリー: 5KBT 5KBU 5KBV
• EMDBエントリー: 8229 8230 8231 8232
• 分子名称: Glutamate receptor 2,Voltage-dependent calcium channel gamma-2 subunit, {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: cryo-em, transport protein
• 由来する生物種: Rattus norvegicus (Rat); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 464585.78

構造登録者

Twomey, E.C.,Yelshanskaya, M.V.,Grassucci, R.A.,Frank, J.,Sobolevsky, A.I. (登録日: 2016-06-03, 公開日: 2016-07-13, 最終更新日: 2024-10-23)

主引用文献

Twomey, E.C.,Yelshanskaya, M.V.,Grassucci, R.A.,Frank, J.,Sobolevsky, A.I.
Elucidation of AMPA receptor-stargazin complexes by cryo-electron microscopy.
Science, 353:83-86, 2016

PubMed Abstract: AMPA-subtype ionotropic glutamate receptors (AMPARs) mediate fast excitatory neurotransmission and contribute to high cognitive processes such as learning and memory. In the brain, AMPAR trafficking, gating, and pharmacology is tightly controlled by transmembrane AMPAR regulatory proteins (TARPs). Here, we used cryo-electron microscopy to elucidate the structural basis of AMPAR regulation by one of these auxiliary proteins, TARP γ2, or stargazin (STZ). Our structures illuminate the variable interaction stoichiometry of the AMPAR-TARP complex, with one or two TARP molecules binding one tetrameric AMPAR. Analysis of the AMPAR-STZ binding interfaces suggests that electrostatic interactions between the extracellular domains of AMPAR and STZ play an important role in modulating AMPAR function through contact surfaces that are conserved across AMPARs and TARPs. We propose a model explaining how TARPs stabilize the activated state of AMPARs and how the interactions between AMPARs and their auxiliary proteins control fast excitatory synaptic transmission.

PubMed: 27365450
DOI: 10.1126/science.aaf8411

実験手法

ELECTRON MICROSCOPY (8.7 Å)