EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Structural mobility tunes signalling of the GluA1 AMPA glutamate receptor.
ジャーナル・号・ページ	Nature, Vol. 621, Issue 7980, Page 877-882, Year 2023
掲載日	2023年9月13日
著者	Danyang Zhang / Josip Ivica / James M Krieger / Hinze Ho / Keitaro Yamashita / Imogen Stockwell / Rozbeh Baradaran / Ondrej Cais / Ingo H Greger /
PubMed 要旨	AMPA glutamate receptors (AMPARs), the primary mediators of excitatory neurotransmission in the brain, are either GluA2 subunit-containing and thus Ca-impermeable, or GluA2-lacking and Ca-permeable. ...AMPA glutamate receptors (AMPARs), the primary mediators of excitatory neurotransmission in the brain, are either GluA2 subunit-containing and thus Ca-impermeable, or GluA2-lacking and Ca-permeable. Despite their prominent expression throughout interneurons and glia, their role in long-term potentiation and their involvement in a range of neuropathologies, structural information for GluA2-lacking receptors is currently absent. Here we determine and characterize cryo-electron microscopy structures of the GluA1 homotetramer, fully occupied with TARPγ3 auxiliary subunits (GluA1/γ3). The gating core of both resting and open-state GluA1/γ3 closely resembles GluA2-containing receptors. However, the sequence-diverse N-terminal domains (NTDs) give rise to a highly mobile assembly, enabling domain swapping and subunit re-alignments in the ligand-binding domain tier that are pronounced in desensitized states. These transitions underlie the unique kinetic properties of GluA1. A GluA2 mutant (F231A) increasing NTD dynamics phenocopies this behaviour, and exhibits reduced synaptic responses, reflecting the anchoring function of the AMPAR NTD at the synapse. Together, this work underscores how the subunit-diverse NTDs determine subunit arrangement, gating properties and ultimately synaptic signalling efficiency among AMPAR subtypes.
リンク	Nature / PubMed:37704721 / PubMed Central
手法	EM (単粒子)
解像度	2.64 - 3.77 Å
構造データ	16379 8c1p EMDB-16379, PDB-8c1p: Active state homomeric GluA1 AMPA receptor in complex with TARP gamma 3 手法: EM (単粒子) / 解像度: 2.9 Å 16380 8c1q EMDB-16380, PDB-8c1q: Resting state homomeric GluA1 AMPA receptor in complex with TARP gamma 3 手法: EM (単粒子) / 解像度: 2.82 Å 16381 8c1r EMDB-16381, PDB-8c1r: Resting state homomeric GluA2 F231A mutant AMPA receptor in complex with TARP gamma-2 手法: EM (単粒子) / 解像度: 3.2 Å 16382 8c1s EMDB-16382, PDB-8c1s: Transmembrane domain of resting state homomeric GluA2 F231A mutant AMPA receptor in complex with TARP gamma 2 手法: EM (単粒子) / 解像度: 3.0 Å 16390 8c2h EMDB-16390, PDB-8c2h: Transmembrane domain of active state homomeric GluA1 AMPA receptor in tandem with TARP gamma 3 手法: EM (単粒子) / 解像度: 2.64 Å 16391 8c2i EMDB-16391, PDB-8c2i: Transmembrane domain of resting state homomeric GluA1 AMPA receptor in complex with TARP gamma 3 手法: EM (単粒子) / 解像度: 2.7 Å 17392 8p3q EMDB-17392, PDB-8p3q: Homomeric GluA2 flip R/G-unedited Q/R-edited F231A mutant in tandem with TARP gamma-2, desensitized conformation 3 手法: EM (単粒子) / 解像度: 2.95 Å 17393 8p3s EMDB-17393, PDB-8p3s: Homomeric GluA2 flip R/G-unedited Q/R-edited F231A mutant in tandem with TARP gamma-2, desensitized conformation 2 手法: EM (単粒子) / 解像度: 2.95 Å 17394 8p3t EMDB-17394, PDB-8p3t: Homomeric GluA1 in tandem with TARP gamma-3, desensitized conformation 1 手法: EM (単粒子) / 解像度: 3.39 Å 17395 8p3u EMDB-17395, PDB-8p3u: Homomeric GluA1 in tandem with TARP gamma-3, desensitized conformation 2 手法: EM (単粒子) / 解像度: 3.77 Å 17396 8p3v EMDB-17396, PDB-8p3v: Homomeric GluA1 in tandem with TARP gamma-3, desensitized conformation 3 手法: EM (単粒子) / 解像度: 3.53 Å 17397 8p3w EMDB-17397, PDB-8p3w: Homomeric GluA1 in tandem with TARP gamma-3, desensitized conformation 4 手法: EM (単粒子) / 解像度: 3.53 Å 17398 8p3x EMDB-17398, PDB-8p3x: Homomeric GluA2 flip R/G-edited Q/R-edited F231A mutant in tandem with TARP gamma-2, desensitized conformation 1 手法: EM (単粒子) / 解像度: 3.36 Å 17399 8p3y EMDB-17399, PDB-8p3y: Homomeric GluA2 flip R/G-edited Q/R-edited F231A mutant in tandem with TARP gamma-2, desensitized conformation 3 手法: EM (単粒子) / 解像度: 3.55 Å 17400 8p3z EMDB-17400, PDB-8p3z: Homomeric GluA2 flip R/G-edited Q/R-edited F231A mutant in tandem with TARP gamma-2, desensitized conformation 2 手法: EM (単粒子) / 解像度: 3.46 Å 17692 8piv EMDB-17692, PDB-8piv: Homomeric GluA2 flip R/G-unedited Q/R-edited F231A mutant in tandem with TARP gamma-2, desensitized conformation 1 手法: EM (単粒子) / 解像度: 3.46 Å
化合物	ChemComp-CYZ: CYCLOTHIAZIDE / (3S)-6-クロロ-3,4-ジヒドロ-3-[(1S,4S,5S)-ビシクロ[2.2.1]ヘプタ-2-エン-5-イル](以下略) ChemComp-PLM: PALMITIC ACID / パルミチン酸 ChemComp-OLC: (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate / L-グリセロ-ル3-オレア-ト ChemComp-GLU: GLUTAMIC ACID / グルタミン酸 ChemComp-POV: (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate / リン脂質YM ChemComp-HOH: WATER ChemComp-ZK1: {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid / ZK-200775 / アンタゴニスト, 薬剤YM
由来	Rattus (ネズミ) rattus norvegicus (ドブネズミ)
キーワード	MEMBRANE PROTEIN / AMPAR / ion channels / neurotransmission / AMPA-type glutamate neurotransmitter receptor / auxiliary subunit complex / agonist / desensitized