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基本情報
登録情報 | データベース: PDB / ID: 5yke | ||||||||||||||||||
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タイトル | Structure of pancreatic ATP-sensitive potassium channel bound with glibenclamide and ATPgammaS (focused refinement on TM at 4.11A) | ||||||||||||||||||
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![]() | MEMBRANE PROTEIN / KATP / channel / glibenclamide / sulfonylurea | ||||||||||||||||||
機能・相同性 | ![]() ATP sensitive Potassium channels / response to resveratrol / ATP-activated inward rectifier potassium channel activity / glutamate secretion, neurotransmission / inward rectifying potassium channel / cell body fiber / Regulation of insulin secretion / sulfonylurea receptor activity / ventricular cardiac muscle tissue development / CAMKK-AMPK signaling cascade ...ATP sensitive Potassium channels / response to resveratrol / ATP-activated inward rectifier potassium channel activity / glutamate secretion, neurotransmission / inward rectifying potassium channel / cell body fiber / Regulation of insulin secretion / sulfonylurea receptor activity / ventricular cardiac muscle tissue development / CAMKK-AMPK signaling cascade / ABC-family proteins mediated transport / voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / response to stress / Ion homeostasis / inward rectifier potassium channel activity / ATPase-coupled monoatomic cation transmembrane transporter activity / nervous system process / regulation of monoatomic ion transmembrane transport / inorganic cation transmembrane transport / neuromuscular process / ankyrin binding / response to ATP / response to testosterone / potassium ion import across plasma membrane / action potential / positive regulation of insulin secretion involved in cellular response to glucose stimulus / potassium ion binding / potassium channel activity / intercalated disc / axolemma / ABC-type transporter activity / cellular response to nutrient levels / negative regulation of insulin secretion / T-tubule / heat shock protein binding / positive regulation of protein localization to plasma membrane / potassium ion transport / acrosomal vesicle / response to ischemia / determination of adult lifespan / cellular response to glucose stimulus / sarcolemma / ADP binding / cellular response to nicotine / glucose metabolic process / nuclear envelope / response to estradiol / cellular response to tumor necrosis factor / presynapse / presynaptic membrane / transmembrane transporter binding / endosome / response to hypoxia / response to xenobiotic stimulus / neuronal cell body / glutamatergic synapse / apoptotic process / ATP hydrolysis activity / ATP binding / plasma membrane / cytoplasm 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: 4.11 Å | ||||||||||||||||||
![]() | Chen, L. / Wu, J.X. | ||||||||||||||||||
資金援助 | ![]()
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![]() | ![]() タイトル: Ligand binding and conformational changes of SUR1 subunit in pancreatic ATP-sensitive potassium channels. 著者: Jing-Xiang Wu / Dian Ding / Mengmeng Wang / Yunlu Kang / Xin Zeng / Lei Chen / ![]() 要旨: ATP-sensitive potassium channels (K) are energy sensors on the plasma membrane. By sensing the intracellular ADP/ATP ratio of β-cells, pancreatic K channels control insulin release and regulate ...ATP-sensitive potassium channels (K) are energy sensors on the plasma membrane. By sensing the intracellular ADP/ATP ratio of β-cells, pancreatic K channels control insulin release and regulate metabolism at the whole body level. They are implicated in many metabolic disorders and diseases and are therefore important drug targets. Here, we present three structures of pancreatic K channels solved by cryo-electron microscopy (cryo-EM), at resolutions ranging from 4.1 to 4.5 Å. These structures depict the binding site of the antidiabetic drug glibenclamide, indicate how Kir6.2 (inward-rectifying potassium channel 6.2) N-terminus participates in the coupling between the peripheral SUR1 (sulfonylurea receptor 1) subunit and the central Kir6.2 channel, reveal the binding mode of activating nucleotides, and suggest the mechanism of how Mg-ADP binding on nucleotide binding domains (NBDs) drives a conformational change of the SUR1 subunit. | ||||||||||||||||||
履歴 |
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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: ![]() ![]() |
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PDBx/mmCIF形式 | ![]() | 813.8 KB | 表示 | ![]() |
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その他 | ![]() |
-検証レポート
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
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-関連構造データ
関連構造データ | ![]() 6831MC ![]() 6832C ![]() 6833C ![]() 6847C ![]() 6848C ![]() 6849C ![]() 6850C ![]() 6851C ![]() 6852C ![]() 6853C ![]() 5ykfC ![]() 5ykgC ![]() 5yw7C ![]() 5yw8C ![]() 5yw9C ![]() 5ywaC ![]() 5ywbC ![]() 5ywcC ![]() 5ywdC 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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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: 43615.734 Da / 分子数: 4 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() #2: タンパク質 | 分子量: 177295.516 Da / 分子数: 4 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() #3: 化合物 | ChemComp-GBM / |
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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: KATP / タイプ: COMPLEX / Entity ID: #1-#2 / 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 | 凍結剤: 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 |
電子銃 | 電子線源: ![]() |
電子レンズ | モード: BRIGHT FIELD |
撮影 | 電子線照射量: 50 e/Å2 フィルム・検出器のモデル: GATAN K2 QUANTUM (4k x 4k) |
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解析
EMソフトウェア | 名称: RELION / バージョン: 2 / カテゴリ: 3次元再構成 |
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CTF補正 | タイプ: NONE |
対称性 | 点対称性: C4 (4回回転対称) |
3次元再構成 | 解像度: 4.11 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 74633 / 対称性のタイプ: POINT |