+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 6njl | |||||||||
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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/IMMUNE SYSTEM / AMPA receptor / ligand gated ion channel / neurotransmitter / synapse / MEMBRANE PROTEIN / MEMBRANE PROTEIN-IMMUNE SYSTEM complex | |||||||||
機能・相同性 | 機能・相同性情報 Presynaptic depolarization and calcium channel opening / Cargo concentration in the ER / cellular response to amine stimulus / axonal spine / 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 / cerebellar mossy fiber ...Presynaptic depolarization and calcium channel opening / Cargo concentration in the ER / cellular response to amine stimulus / axonal spine / 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 / cerebellar mossy fiber / neurotransmitter receptor transport, postsynaptic endosome to lysosome / LGI-ADAM interactions / myosin V binding / neurotransmitter receptor activity involved in regulation of postsynaptic cytosolic calcium ion concentration / Trafficking of AMPA receptors / neuron spine / regulation of AMPA receptor activity / neurotransmitter receptor internalization / response to arsenic-containing substance / membrane hyperpolarization / cellular response to dsRNA / postsynaptic neurotransmitter receptor diffusion trapping / nervous system process / dendritic spine membrane / Synaptic adhesion-like molecules / protein targeting to membrane / long-term synaptic depression / beta-2 adrenergic receptor binding / cellular response to peptide hormone stimulus / voltage-gated calcium channel complex / neurotransmitter receptor localization to postsynaptic specialization membrane / protein kinase A binding / neuromuscular junction development / spinal cord development / spine synapse / dendritic spine neck / neuronal cell body membrane / dendritic spine head / Activation of AMPA receptors / perisynaptic space / transmission of nerve impulse / AMPA glutamate receptor activity / channel regulator activity / ligand-gated monoatomic cation channel activity / Trafficking of GluR2-containing AMPA receptors / response to lithium ion / regulation of postsynaptic membrane neurotransmitter receptor levels / immunoglobulin binding / membrane depolarization / AMPA glutamate receptor complex / adenylate cyclase binding / kainate selective glutamate receptor activity / cellular response to organic cyclic compound / ionotropic glutamate receptor complex / excitatory synapse / extracellularly glutamate-gated ion channel activity / neuronal action potential / cellular response to glycine / calcium channel regulator activity / asymmetric synapse / G-protein alpha-subunit binding / regulation of receptor recycling / voltage-gated calcium channel activity / regulation of postsynaptic membrane potential / Unblocking of NMDA receptors, glutamate binding and activation / postsynaptic density, intracellular component / positive regulation of synaptic transmission / glutamate receptor binding / long-term memory / extracellular ligand-gated monoatomic ion channel activity / positive regulation of synaptic transmission, glutamatergic / response to electrical stimulus / glutamate-gated receptor activity / glutamate-gated calcium ion channel activity / presynaptic active zone membrane / response to fungicide / regulation of synaptic transmission, glutamatergic / somatodendritic compartment / synapse assembly / cellular response to brain-derived neurotrophic factor stimulus / dendrite membrane / ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / cytoskeletal protein binding / ionotropic glutamate receptor binding / dendrite cytoplasm / ionotropic glutamate receptor signaling pathway / hippocampal mossy fiber to CA3 synapse / cellular response to amino acid stimulus / regulation of membrane potential / SNARE binding / response to cocaine / dendritic shaft / transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / synaptic membrane / synaptic transmission, glutamatergic / PDZ domain binding / long-term synaptic potentiation / protein tetramerization / postsynaptic density membrane / response to calcium ion 類似検索 - 分子機能 | |||||||||
生物種 | Mus musculus (ハツカネズミ) Rattus norvegicus (ドブネズミ) | |||||||||
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: 6.7 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. | |||||||||
履歴 |
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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: MolmilJmol/JSmol |
-ダウンロードとリンク
-ダウンロード
PDBx/mmCIF形式 | 6njl.cif.gz | 851.3 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb6njl.ent.gz | 668.4 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 6njl.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 | 6njl_validation.pdf.gz | 1.4 MB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 6njl_full_validation.pdf.gz | 1.4 MB | 表示 | |
XML形式データ | 6njl_validation.xml.gz | 115.6 KB | 表示 | |
CIF形式データ | 6njl_validation.cif.gz | 182.5 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/nj/6njl ftp://data.pdbj.org/pub/pdb/validation_reports/nj/6njl | HTTPS FTP |
-関連構造データ
関連構造データ | 9387MC 0426C 0427C 0428C 0429C 0430C 0431C 0432C 9388C 9389C 6njmC 6njnC 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 (文献) |
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類似構造データ |
-リンク
-集合体
登録構造単位 |
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-要素
-Glutamate receptor ... , 2種, 4分子 ACBD
#1: タンパク質 | 分子量: 101518.773 Da / 分子数: 2 / 由来タイプ: 天然 / 由来: (天然) Rattus norvegicus (ドブネズミ) / 参照: UniProt: P19490 #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) Rattus norvegicus (ドブネズミ) / 参照: UniProt: P19491 |
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-タンパク質 , 2種, 4分子 EGFH
#3: タンパク質 | 分子量: 13039.064 Da / 分子数: 2 / 由来タイプ: 天然 / 由来: (天然) Rattus norvegicus (ドブネズミ) #4: 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) Rattus norvegicus (ドブネズミ) / 参照: UniProt: Q71RJ2 |
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-抗体 , 3種, 6分子 ILJMKN
#5: 抗体 | 分子量: 27511.527 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) Mus musculus (ハツカネズミ) 発現宿主: Spodoptera frugiperda (ツマジロクサヨトウ) #6: 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) Mus musculus (ハツカネズミ) 発現宿主: Spodoptera frugiperda (ツマジロクサヨトウ) #7: 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) Mus musculus (ハツカネズミ) 発現宿主: Spodoptera frugiperda (ツマジロクサヨトウ) |
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-糖 , 2種, 12分子
#8: 多糖 | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose #10: 糖 | ChemComp-NAG / |
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-非ポリマー , 1種, 4分子
#9: 化合物 | ChemComp-ZK1 / {[ |
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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 |
-試料調製
構成要素 | 名称: Native A1A2A1A2 complex bound with MPQX / タイプ: COMPLEX / Entity ID: #1-#7 / 由来: NATURAL | ||||||||||||||||||||
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由来(天然) | 生物種: Rattus norvegicus (ドブネズミ) | ||||||||||||||||||||
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 |
-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) |
-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: 6.7 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 130000 / 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 | ||||||||||||||||||
精密化 | 最高解像度: 6.7 Å |