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基本情報
登録情報 | データベース: PDB / ID: 6njn | |||||||||
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タイトル | Architecture and subunit arrangement of native AMPA receptors | |||||||||
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![]() | MEMBRANE PROTEIN / AMPA receptor / ligand gated ion channel / neurotransmitter / synapse | |||||||||
機能・相同性 | ![]() Presynaptic depolarization and calcium channel opening / chemical synaptic transmission, postsynaptic / Cargo concentration in the ER / cellular response to amine stimulus / axonal spine / eye blink reflex / positive regulation of protein localization to basolateral plasma membrane / COPII-mediated vesicle transport / positive regulation of membrane potential / cellular response to ammonium ion ...Presynaptic depolarization and calcium channel opening / chemical synaptic transmission, postsynaptic / Cargo concentration in the ER / cellular response to amine stimulus / axonal spine / eye blink reflex / positive regulation of protein localization to basolateral plasma membrane / COPII-mediated vesicle transport / positive regulation of membrane potential / cellular response to ammonium ion / cerebellar mossy fiber / neurotransmitter receptor transport, postsynaptic endosome to lysosome / neurotransmitter receptor activity involved in regulation of postsynaptic cytosolic calcium ion concentration / LGI-ADAM interactions / myosin V binding / Trafficking of AMPA receptors / neuron spine / regulation of AMPA receptor activity / neurotransmitter receptor internalization / channel regulator activity / membrane hyperpolarization / response to arsenic-containing substance / cellular response to dsRNA / postsynaptic neurotransmitter receptor diffusion trapping / dendritic spine membrane / Synaptic adhesion-like molecules / nervous system process / glutamate-gated calcium ion channel activity / parallel fiber to Purkinje cell synapse / protein targeting to membrane / neurotransmitter receptor localization to postsynaptic specialization membrane / long-term synaptic depression / cellular response to peptide hormone stimulus / voltage-gated calcium channel complex / protein kinase A binding / neuromuscular junction development / spinal cord development / spine synapse / neuronal cell body membrane / dendritic spine neck / dendritic spine head / Activation of AMPA receptors / perisynaptic space / transmission of nerve impulse / AMPA glutamate receptor activity / regulation of postsynaptic membrane neurotransmitter receptor levels / Trafficking of GluR2-containing AMPA receptors / response to lithium ion / immunoglobulin binding / membrane depolarization / AMPA glutamate receptor complex / kainate selective glutamate receptor activity / cellular response to organic cyclic compound / adenylate cyclase binding / ionotropic glutamate receptor complex / extracellularly glutamate-gated ion channel activity / cellular response to glycine / excitatory synapse / calcium channel regulator activity / asymmetric synapse / regulation of receptor recycling / G-protein alpha-subunit binding / voltage-gated calcium channel activity / Unblocking of NMDA receptors, glutamate binding and activation / neuronal action potential / regulation of postsynaptic membrane potential / postsynaptic density, intracellular component / glutamate receptor binding / positive regulation of synaptic transmission / long-term memory / response to electrical stimulus / synaptic cleft / glutamate-gated receptor activity / presynaptic active zone membrane / beta-2 adrenergic receptor binding / response to fungicide / monoatomic ion transmembrane transport / regulation of synaptic transmission, glutamatergic / somatodendritic compartment / cellular response to brain-derived neurotrophic factor stimulus / dendrite membrane / synapse assembly / ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / cytoskeletal protein binding / ionotropic glutamate receptor signaling pathway / dendrite cytoplasm / hippocampal mossy fiber to CA3 synapse / positive regulation of synaptic transmission, glutamatergic / SNARE binding / response to cocaine / dendritic shaft / synaptic membrane / synaptic transmission, glutamatergic / transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / PDZ domain binding / regulation of membrane potential / long-term synaptic potentiation / protein tetramerization / cellular response to amino acid stimulus / postsynaptic density membrane 類似検索 - 分子機能 | |||||||||
生物種 | ![]() ![]() ![]() ![]() | |||||||||
手法 | 電子顕微鏡法 / 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 6.5 Å | |||||||||
![]() | Gouaux, E. / Zhao, Y. | |||||||||
![]() | ![]() タイトル: Architecture and subunit arrangement of native AMPA receptors elucidated by cryo-EM. 著者: Yan Zhao / Shanshuang Chen / Adam C Swensen / Wei-Jun Qian / Eric Gouaux / ![]() 要旨: 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 ...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. | |||||||||
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構造ビューア | 分子: ![]() ![]() |
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PDBx/mmCIF形式 | ![]() | 876.8 KB | 表示 | ![]() |
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PDB形式 | ![]() | 689.7 KB | 表示 | ![]() |
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-検証レポート
文書・要旨 | ![]() | 1.6 MB | 表示 | ![]() |
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文書・詳細版 | ![]() | 1.6 MB | 表示 | |
XML形式データ | ![]() | 119.8 KB | 表示 | |
CIF形式データ | ![]() | 188.2 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
関連構造データ | ![]() 9389MC ![]() 0426C ![]() 0427C ![]() 0428C ![]() 0429C ![]() 0430C ![]() 0431C ![]() 0432C ![]() 9387C ![]() 9388C ![]() 6njlC ![]() 6njmC M: このデータのモデリングに利用したマップデータ C: 同じ文献を引用 ( |
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集合体
登録構造単位 | ![]()
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要素
-Glutamate receptor ... , 3種, 4分子 ABDC
#1: タンパク質 | 分子量: 101518.773 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) ![]() ![]() | ||
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#2: タンパク質 | 分子量: 98783.805 Da / 分子数: 2 / 由来タイプ: 天然 / 由来: (天然) ![]() ![]() #3: タンパク質 | | 分子量: 100556.680 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) ![]() ![]() |
-抗体 , 5種, 9分子 EGIJNKOLM
#4: 抗体 | 分子量: 13039.064 Da / 分子数: 2 / 由来タイプ: 天然 / 由来: (天然) ![]() ![]() #6: 抗体 | | 分子量: 27511.527 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() ![]() #7: 抗体 | 分子量: 25111.660 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() 発現宿主: ![]() ![]() #8: 抗体 | 分子量: 27975.439 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() 発現宿主: ![]() ![]() #9: 抗体 | 分子量: 19081.451 Da / 分子数: 2 / 由来タイプ: 天然 / 由来: (天然) ![]() ![]() |
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-タンパク質 / 非ポリマー , 2種, 6分子 FH![](data/chem/img/ZK1.gif)
![](data/chem/img/ZK1.gif)
#12: 化合物 | ChemComp-ZK1 / {[ #5: タンパク質 | 分子量: 35938.746 Da / 分子数: 2 / 由来タイプ: 天然 / 由来: (天然) ![]() ![]() |
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-糖 , 3種, 11分子 ![](data/chem/img/NAG.gif)
#10: 多糖 | beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose #11: 多糖 | #13: 糖 | |
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-実験情報
-実験
実験 | 手法: 電子顕微鏡法 |
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EM実験 | 試料の集合状態: PARTICLE / 3次元再構成法: 単粒子再構成法 |
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試料調製
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由来(天然) |
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緩衝液 | pH: 8 | ||||||||||||||||||||||||||||||
緩衝液成分 |
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試料 | 濃度: 4 mg/ml / 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES | ||||||||||||||||||||||||||||||
試料支持 | 詳細: unspecified | ||||||||||||||||||||||||||||||
急速凍結 | 凍結剤: ETHANE / 湿度: 100 % / 凍結前の試料温度: 295 K |
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電子顕微鏡撮影
実験機器 | ![]() モデル: Titan Krios / 画像提供: FEI Company |
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顕微鏡 | モデル: FEI TITAN KRIOS |
電子銃 | 電子線源: ![]() |
電子レンズ | モード: BRIGHT FIELD |
撮影 | 電子線照射量: 54 e/Å2 / 検出モード: SUPER-RESOLUTION フィルム・検出器のモデル: GATAN K2 SUMMIT (4k x 4k) |
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解析
EMソフトウェア |
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CTF補正 | タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||
3次元再構成 | 解像度: 6.5 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 161000 / 対称性のタイプ: POINT | ||||||||||||||||||
原子モデル構築 | プロトコル: RIGID BODY FIT / 空間: REAL |