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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: 4uq6 | ||||||
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| タイトル | Electron density map of GluA2em in complex with LY451646 and glutamate | ||||||
要素 | GLUTAMATE RECEPTOR 2 | ||||||
キーワード | TRANSPORT PROTEIN / MEMBRANE PROTEIN / ION CHANNEL | ||||||
| 機能・相同性 | 機能・相同性情報spine synapse / dendritic spine neck / dendritic spine cytoplasm / cellular response to amine stimulus / dendritic spine head / Activation of AMPA receptors / perisynaptic space / ligand-gated monoatomic cation channel activity / Trafficking of GluR2-containing AMPA receptors / response to lithium ion ...spine synapse / dendritic spine neck / dendritic spine cytoplasm / cellular response to amine stimulus / dendritic spine head / Activation of AMPA receptors / perisynaptic space / ligand-gated monoatomic cation channel activity / Trafficking of GluR2-containing AMPA receptors / response to lithium ion / AMPA glutamate receptor activity / AMPA glutamate receptor clustering / kainate selective glutamate receptor activity / immunoglobulin binding / asymmetric synapse / AMPA glutamate receptor complex / regulation of receptor recycling / extracellularly glutamate-gated ion channel activity / cellular response to glycine / ionotropic glutamate receptor complex / Unblocking of NMDA receptors, glutamate binding and activation / glutamate receptor binding / conditioned place preference / positive regulation of synaptic transmission / response to fungicide / regulation of synaptic transmission, glutamatergic / glutamate-gated receptor activity / extracellular ligand-gated monoatomic ion channel activity / cytoskeletal protein binding / cellular response to brain-derived neurotrophic factor stimulus / regulation of long-term synaptic depression / somatodendritic compartment / glutamate-gated calcium ion channel activity / presynaptic active zone membrane / excitatory synapse / ionotropic glutamate receptor signaling pathway / ionotropic glutamate receptor binding / dendrite membrane / ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / dendrite cytoplasm / positive regulation of excitatory postsynaptic potential / dendritic shaft / synaptic membrane / SNARE binding / PDZ domain binding / synaptic transmission, glutamatergic / establishment of protein localization / protein tetramerization / transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / cerebral cortex development / receptor internalization / postsynaptic density membrane / modulation of chemical synaptic transmission / Schaffer collateral - CA1 synapse / terminal bouton / synaptic vesicle / long-term synaptic potentiation / amyloid-beta binding / synaptic vesicle membrane / presynapse / growth cone / signaling receptor activity / presynaptic membrane / scaffold protein binding / dendritic spine / chemical synaptic transmission / perikaryon / postsynaptic membrane / neuron projection / postsynaptic density / external side of plasma membrane / axon / neuronal cell body / synapse / dendrite / protein kinase binding / protein-containing complex binding / glutamatergic synapse / cell surface / endoplasmic reticulum / protein-containing complex / membrane / identical protein binding / plasma 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: 12.8 Å | ||||||
データ登録者 | Meyerson, J.R. / Kumar, J. / Chittori, S. / Rao, P. / Pierson, J. / Bartesaghi, A. / Mayer, M.L. / Subramaniam, S. | ||||||
引用 | ジャーナル: Nature / 年: 2014タイトル: Structural mechanism of glutamate receptor activation and desensitization. 著者: Joel R Meyerson / Janesh Kumar / Sagar Chittori / Prashant Rao / Jason Pierson / Alberto Bartesaghi / Mark L Mayer / Sriram Subramaniam / ![]() 要旨: Ionotropic glutamate receptors are ligand-gated ion channels that mediate excitatory synaptic transmission in the vertebrate brain. To gain a better understanding of how structural changes gate ion ...Ionotropic glutamate receptors are ligand-gated ion channels that mediate excitatory synaptic transmission in the vertebrate brain. To gain a better understanding of how structural changes gate ion flux across the membrane, we trapped rat AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid) and kainate receptor subtypes in their major functional states and analysed the resulting structures using cryo-electron microscopy. We show that transition to the active state involves a 'corkscrew' motion of the receptor assembly, driven by closure of the ligand-binding domain. Desensitization is accompanied by disruption of the amino-terminal domain tetramer in AMPA, but not kainate, receptors with a two-fold to four-fold symmetry transition in the ligand-binding domains in both subtypes. The 7.6 Å structure of a desensitized kainate receptor shows how these changes accommodate channel closing. These findings integrate previous physiological, biochemical and structural analyses of glutamate receptors and provide a molecular explanation for key steps in receptor 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 | 4uq6.cif.gz | 419.8 KB | 表示 | PDBx/mmCIF形式 |
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| PDB形式 | pdb4uq6.ent.gz | 323.9 KB | 表示 | PDB形式 |
| PDBx/mmJSON形式 | 4uq6.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/uq/4uq6 ftp://data.pdbj.org/pub/pdb/validation_reports/uq/4uq6 | HTTPS FTP |
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-関連構造データ
| 関連構造データ | ![]() 2684MC ![]() 2680C ![]() 2685C ![]() 2686C ![]() 2687C ![]() 2688C ![]() 2689C ![]() 4uqjC ![]() 4uqkC ![]() 4uqqC C: 同じ文献を引用 ( M: このデータのモデリングに利用したマップデータ |
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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
| #1: タンパク質 | 分子量: 92625.578 Da / 分子数: 4 / 断片: RESIDUES 22-847 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() 発現宿主: ![]() 参照: UniProt: P19491 #2: 化合物 | ChemComp-GLU / 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 | 名称: GLUA2 / タイプ: COMPLEX |
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| 緩衝液 | pH: 8 |
| 試料 | 濃度: 1.8 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: HOLEY CARBON |
| 急速凍結 | 装置: FEI VITROBOT MARK IV / 凍結剤: ETHANE / 詳細: ETHANE |
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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 / 日付: 2013年8月1日 |
| 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 / 倍率(公称値): 47000 X / 倍率(補正後): 47000 X / 最大 デフォーカス(公称値): 3500 nm / 最小 デフォーカス(公称値): 2000 nm |
| 撮影 | 電子線照射量: 25 e/Å2 フィルム・検出器のモデル: FEI FALCON II (4k x 4k) |
| 画像スキャン | デジタル画像の数: 1566 |
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解析
| EMソフトウェア |
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| CTF補正 | 詳細: EACH PARTICLE | |||||||||||||||||||||
| 対称性 | 点対称性: C2 (2回回転対称) | |||||||||||||||||||||
| 3次元再構成 | 解像度: 12.8 Å / 粒子像の数: 16050 詳細: SUBMISSION BASED ON EXPERIMENTAL DATA FROM EMDB EMD-2684. (DEPOSITION ID: 12579). 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 / 詳細: METHOD--RIGID BODY REFINEMENT PROTOCOL--X-RAY | |||||||||||||||||||||
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| 精密化 | 最高解像度: 12.8 Å | |||||||||||||||||||||
| 精密化ステップ | サイクル: LAST / 最高解像度: 12.8 Å
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