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データを開く
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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 | ||||||||||||
要素 |
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キーワード | MEMBRANE PROTEIN / AMPA receptor / ligand gated ion channel / neurotransmitter / synapse | ||||||||||||
| 機能・相同性 | 機能・相同性情報Cargo concentration in the ER / Presynaptic depolarization and calcium channel opening / axonal spine / positive regulation of locomotion involved in locomotory behavior / COPII-mediated vesicle transport / positive regulation of membrane potential / eye blink reflex / positive regulation of protein localization to basolateral plasma membrane / cellular response to ammonium ion / response to sucrose ...Cargo concentration in the ER / Presynaptic depolarization and calcium channel opening / axonal spine / positive regulation of locomotion involved in locomotory behavior / COPII-mediated vesicle transport / positive regulation of membrane potential / eye blink reflex / positive regulation of protein localization to basolateral plasma membrane / cellular response to ammonium ion / response to sucrose / myosin V binding / cerebellar mossy fiber / LGI-ADAM interactions / neuron spine / Trafficking of AMPA receptors / postsynaptic neurotransmitter receptor diffusion trapping / proximal dendrite / regulation of AMPA receptor activity / response to arsenic-containing substance / regulation of monoatomic ion transmembrane transport / channel regulator activity / cellular response to L-glutamate / cellular response to dsRNA / membrane hyperpolarization / ligand-gated calcium channel activity / dendritic spine membrane / nervous system process / Synaptic adhesion-like molecules / beta-2 adrenergic receptor binding / long-term synaptic depression / protein targeting to membrane / cellular response to peptide hormone stimulus / voltage-gated calcium channel complex / spine synapse / dendritic spine neck / dendritic spine cytoplasm / dendritic spine head / cellular response to amine stimulus / peptide hormone receptor binding / response to psychosocial stress / protein heterotetramerization / response to morphine / Activation of AMPA receptors / neurotransmitter receptor localization to postsynaptic specialization membrane / ligand-gated monoatomic cation channel activity / spinal cord development / perisynaptic space / neuronal cell body membrane / protein kinase A binding / neuromuscular junction development / Trafficking of GluR2-containing AMPA receptors / parallel fiber to Purkinje cell synapse / response to lithium ion / AMPA glutamate receptor activity / AMPA glutamate receptor clustering / transmission of nerve impulse / kainate selective glutamate receptor activity / behavioral response to pain / immunoglobulin binding / adenylate cyclase binding / asymmetric synapse / response to electrical stimulus / extracellularly glutamate-gated ion channel activity / AMPA glutamate receptor complex / cellular response to glycine / regulation of receptor recycling / membrane depolarization / ionotropic glutamate receptor complex / Unblocking of NMDA receptors, glutamate binding and activation / G-protein alpha-subunit binding / glutamate receptor binding / conditioned place preference / positive regulation of synaptic transmission / long-term memory / regulation of postsynaptic membrane neurotransmitter receptor levels / voltage-gated calcium channel activity / postsynaptic density, intracellular component / synaptic cleft / response to fungicide / regulation of synaptic transmission, glutamatergic / neuronal action potential / positive regulation of synaptic transmission, glutamatergic / extracellular ligand-gated monoatomic ion channel activity / cytoskeletal protein binding / glutamate-gated receptor activity / regulation of long-term synaptic depression / cellular response to brain-derived neurotrophic factor stimulus / somatodendritic compartment / glutamate-gated calcium ion channel activity / presynaptic active zone membrane / synapse assembly / excitatory synapse / ionotropic glutamate receptor signaling pathway / ionotropic glutamate receptor binding / dendrite membrane / dendrite cytoplasm / ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / positive regulation of excitatory postsynaptic potential / hippocampal mossy fiber to CA3 synapse / dendritic shaft 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 | ||||||||||||
データ登録者 | Gouaux, E. / Zhao, Y. | ||||||||||||
引用 | ジャーナル: Science / 年: 2019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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構造の表示
| ムービー |
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| 構造ビューア | 分子: Molmil Jmol/JSmol |
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ダウンロードとリンク
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ダウンロード
| PDBx/mmCIF形式 | 6njn.cif.gz | 883 KB | 表示 | PDBx/mmCIF形式 |
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| PDB形式 | pdb6njn.ent.gz | 675.4 KB | 表示 | PDB形式 |
| PDBx/mmJSON形式 | 6njn.json.gz | ツリー表示 | PDBx/mmJSON形式 | |
| その他 | その他のダウンロード |
-検証レポート
| アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/nj/6njn ftp://data.pdbj.org/pub/pdb/validation_reports/nj/6njn | HTTPS FTP |
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-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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| 類似構造データ |
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リンク
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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

| #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 
| #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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-詳細
| Has protein modification | Y |
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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: FIELD EMISSION GUN / 加速電圧: 300 kV / 照射モード: FLOOD BEAM |
| 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 |
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