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基本情報
登録情報 | データベース: PDB / ID: 8sda | ||||||
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タイトル | CryoEM structure of rat Kv2.1(1-598) L403A mutant in nanodiscs | ||||||
![]() | Potassium voltage-gated channel subfamily B member 1 | ||||||
![]() | MEMBRANE PROTEIN / voltage-dependent potassium channel | ||||||
機能・相同性 | ![]() regulation of action potential / clustering of voltage-gated potassium channels / positive regulation of long-term synaptic depression / regulation of motor neuron apoptotic process / Voltage gated Potassium channels / positive regulation of norepinephrine secretion / positive regulation of catecholamine secretion / potassium ion export across plasma membrane / proximal dendrite / cholinergic synapse ...regulation of action potential / clustering of voltage-gated potassium channels / positive regulation of long-term synaptic depression / regulation of motor neuron apoptotic process / Voltage gated Potassium channels / positive regulation of norepinephrine secretion / positive regulation of catecholamine secretion / potassium ion export across plasma membrane / proximal dendrite / cholinergic synapse / positive regulation of calcium ion-dependent exocytosis / Glucagon-like Peptide-1 (GLP1) regulates insulin secretion / delayed rectifier potassium channel activity / vesicle docking involved in exocytosis / glutamate receptor signaling pathway / outward rectifier potassium channel activity / postsynaptic specialization membrane / response to L-glutamate / action potential / neuronal cell body membrane / voltage-gated potassium channel activity / cellular response to nutrient levels / lateral plasma membrane / response to axon injury / positive regulation of protein targeting to membrane / negative regulation of insulin secretion / potassium ion transmembrane transport / voltage-gated potassium channel complex / dendrite membrane / cellular response to calcium ion / SNARE binding / protein localization to plasma membrane / cellular response to glucose stimulus / potassium ion transport / protein homooligomerization / sarcolemma / glucose homeostasis / postsynaptic membrane / perikaryon / transmembrane transporter binding / apical plasma membrane / protein heterodimerization activity / axon / neuronal cell body / dendrite / perinuclear region of cytoplasm / cell surface / 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: 3.32 Å | ||||||
![]() | Tan, X. / Swartz, K.J. | ||||||
資金援助 | ![]()
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![]() | ![]() タイトル: Inactivation of the Kv2.1 channel through electromechanical coupling. 著者: Ana I Fernández-Mariño / Xiao-Feng Tan / Chanhyung Bae / Kate Huffer / Jiansen Jiang / Kenton J Swartz / ![]() 要旨: The Kv2.1 voltage-activated potassium (Kv) channel is a prominent delayed-rectifier Kv channel in the mammalian central nervous system, where its mechanisms of activation and inactivation are ...The Kv2.1 voltage-activated potassium (Kv) channel is a prominent delayed-rectifier Kv channel in the mammalian central nervous system, where its mechanisms of activation and inactivation are critical for regulating intrinsic neuronal excitability. Here we present structures of the Kv2.1 channel in a lipid environment using cryo-electron microscopy to provide a framework for exploring its functional mechanisms and how mutations causing epileptic encephalopathies alter channel activity. By studying a series of disease-causing mutations, we identified one that illuminates a hydrophobic coupling nexus near the internal end of the pore that is critical for inactivation. Both functional and structural studies reveal that inactivation in Kv2.1 results from dynamic alterations in electromechanical coupling to reposition pore-lining S6 helices and close the internal pore. Consideration of these findings along with available structures for other Kv channels, as well as voltage-activated sodium and calcium channels, suggests that related mechanisms of inactivation are conserved in voltage-activated cation channels and likely to be engaged by widely used therapeutics to achieve state-dependent regulation of channel activity. | ||||||
履歴 |
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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PDBx/mmCIF形式 | ![]() | 203 KB | 表示 | ![]() |
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PDB形式 | ![]() | 144.2 KB | 表示 | ![]() |
PDBx/mmJSON形式 | ![]() | ツリー表示 | ![]() | |
その他 | ![]() |
-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 | ![]() | 43.1 KB | 表示 | |
CIF形式データ | ![]() | 58.2 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 | ![]() 40350MC ![]() 8sd3C 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 | 類似検索 - 機能・相同性 ![]() |
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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: 68550.023 Da / 分子数: 4 / 変異: L403A / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() #2: 化合物 | ChemComp-POV / ( #3: 化合物 | ChemComp-K / 研究の焦点であるリガンドがあるか | N | |
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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: Voltage-dependent potassium channel Kv2.1 L403A mutant タイプ: COMPLEX / Entity ID: #1 / 由来: RECOMBINANT |
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由来(天然) | 生物種: ![]() ![]() |
由来(組換発現) | 生物種: ![]() |
緩衝液 | pH: 7.5 |
試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES |
急速凍結 | 装置: FEI VITROBOT MARK IV / 凍結剤: ETHANE / 湿度: 100 % |
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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: TUNGSTEN HAIRPIN / 加速電圧: 300 kV / 照射モード: FLOOD BEAM |
電子レンズ | モード: BRIGHT FIELD / 最大 デフォーカス(公称値): 1500 nm / 最小 デフォーカス(公称値): 500 nm |
撮影 | 電子線照射量: 48 e/Å2 フィルム・検出器のモデル: GATAN K3 BIOQUANTUM (6k x 4k) |
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解析
ソフトウェア |
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CTF補正 | タイプ: NONE | ||||||||||||||||||||||||
3次元再構成 | 解像度: 3.32 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 505078 / 対称性のタイプ: POINT | ||||||||||||||||||||||||
原子モデル構築 | プロトコル: RIGID BODY FIT | ||||||||||||||||||||||||
精密化 | 交差検証法: NONE 立体化学のターゲット値: GeoStd + Monomer Library + CDL v1.2 | ||||||||||||||||||||||||
原子変位パラメータ | Biso mean: 73.61 Å2 | ||||||||||||||||||||||||
拘束条件 |
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