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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 / axonal spine / Presynaptic depolarization and calcium channel opening / positive regulation of locomotion involved in locomotory behavior / positive regulation of membrane potential / COPII-mediated vesicle transport / 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 / axonal spine / Presynaptic depolarization and calcium channel opening / positive regulation of locomotion involved in locomotory behavior / positive regulation of membrane potential / COPII-mediated vesicle transport / eye blink reflex / positive regulation of protein localization to basolateral plasma membrane / cellular response to ammonium ion / response to sucrose / neuron spine / myosin V binding / cerebellar mossy fiber / postsynaptic neurotransmitter receptor diffusion trapping / proximal dendrite / regulation of monoatomic ion transmembrane transport / regulation of AMPA receptor activity / channel regulator activity / Trafficking of AMPA receptors / LGI-ADAM interactions / response to arsenic-containing substance / cellular response to L-glutamate / cellular response to dsRNA / dendritic spine membrane / membrane hyperpolarization / long-term synaptic depression / nervous system process / beta-2 adrenergic receptor binding / Synaptic adhesion-like molecules / protein targeting to membrane / cellular response to peptide hormone stimulus / voltage-gated calcium channel complex / response to morphine / neuronal cell body membrane / spine synapse / dendritic spine neck / protein kinase A binding / dendritic spine head / protein heterotetramerization / peptide hormone receptor binding / cellular response to amine stimulus / neurotransmitter receptor localization to postsynaptic specialization membrane / response to psychosocial stress / spinal cord development / neuromuscular junction development / perisynaptic space / Activation of AMPA receptors / parallel fiber to Purkinje cell synapse / ligand-gated monoatomic cation channel activity / AMPA glutamate receptor activity / transmission of nerve impulse / response to lithium ion / Trafficking of GluR2-containing AMPA receptors / behavioral response to pain / kainate selective glutamate receptor activity / AMPA glutamate receptor complex / cellular response to glycine / adenylate cyclase binding / extracellularly glutamate-gated ion channel activity / immunoglobulin binding / asymmetric synapse / ionotropic glutamate receptor complex / conditioned place preference / excitatory synapse / response to electrical stimulus / regulation of receptor recycling / G-protein alpha-subunit binding / membrane depolarization / glutamate receptor binding / Unblocking of NMDA receptors, glutamate binding and activation / positive regulation of excitatory postsynaptic potential / long-term memory / positive regulation of synaptic transmission / synaptic cleft / positive regulation of synaptic transmission, glutamatergic / postsynaptic density, intracellular component / regulation of postsynaptic membrane neurotransmitter receptor levels / regulation of synaptic transmission, glutamatergic / neuronal action potential / voltage-gated calcium channel activity / response to fungicide / cytoskeletal protein binding / glutamate-gated receptor activity / synapse assembly / regulation of long-term synaptic depression / extracellular ligand-gated monoatomic ion channel activity / cellular response to brain-derived neurotrophic factor stimulus / presynaptic active zone membrane / glutamate-gated calcium ion channel activity / somatodendritic compartment / dendrite membrane / ionotropic glutamate receptor binding / ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / ionotropic glutamate receptor signaling pathway / dendrite cytoplasm / synaptic membrane / hippocampal mossy fiber to CA3 synapse / dendritic shaft / SNARE binding / regulation of membrane potential 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 | 
 
  ムービービューア | 
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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
| 文書・要旨 |  6njn_validation.pdf.gz | 1.6 MB | 表示 |  wwPDB検証レポート | 
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| 文書・詳細版 |  6njn_full_validation.pdf.gz | 1.7 MB | 表示 | |
| XML形式データ |  6njn_validation.xml.gz | 119.5 KB | 表示 | |
| CIF形式データ |  6njn_validation.cif.gz | 188.2 KB | 表示 | |
| 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  | 
-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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| 1 | 
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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
| 構成要素 | 
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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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