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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: 1y4e | ||||||
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タイトル | NMR structure of transmembrane segment IV of the NHE1 isoform of the Na+/H+ exchanger | ||||||
![]() | Sodium/hydrogen exchanger 1 | ||||||
![]() | MEMBRANE PROTEIN / NHE1 isoform / transmembrane | ||||||
機能・相同性 | ![]() sodium:proton antiporter activity involved in regulation of cardiac muscle cell membrane potential / cation-transporting ATPase complex / Sodium/Proton exchangers / regulation of the force of heart contraction by cardiac conduction / positive regulation of calcium:sodium antiporter activity / Hyaluronan uptake and degradation / regulation of cardiac muscle cell membrane potential / cellular response to electrical stimulus / potassium:proton antiporter activity / sodium:proton antiporter activity ...sodium:proton antiporter activity involved in regulation of cardiac muscle cell membrane potential / cation-transporting ATPase complex / Sodium/Proton exchangers / regulation of the force of heart contraction by cardiac conduction / positive regulation of calcium:sodium antiporter activity / Hyaluronan uptake and degradation / regulation of cardiac muscle cell membrane potential / cellular response to electrical stimulus / potassium:proton antiporter activity / sodium:proton antiporter activity / positive regulation of action potential / maintenance of cell polarity / positive regulation of calcineurin-NFAT signaling cascade / regulation of pH / sodium ion export across plasma membrane / cellular response to acidic pH / cardiac muscle cell differentiation / ion binding / sodium ion import across plasma membrane / protein phosphatase 2B binding / intracellular sodium ion homeostasis / cardiac muscle cell contraction / response to acidic pH / regulation of stress fiber assembly / regulation of cardiac muscle contraction by calcium ion signaling / positive regulation of mitochondrial membrane permeability / cellular response to cold / cellular response to antibiotic / regulation of focal adhesion assembly / positive regulation of cardiac muscle hypertrophy / positive regulation of the force of heart contraction / cellular response to organic cyclic compound / intercalated disc / monoatomic ion transport / potassium ion transmembrane transport / proton transmembrane transport / T-tubule / cellular response to epinephrine stimulus / response to muscle stretch / phosphatidylinositol-4,5-bisphosphate binding / stem cell differentiation / regulation of intracellular pH / phospholipid binding / cellular response to mechanical stimulus / cellular response to insulin stimulus / calcium-dependent protein binding / cell migration / lamellipodium / protein complex oligomerization / protein-macromolecule adaptor activity / cellular response to hypoxia / positive regulation of cell growth / basolateral plasma membrane / molecular adaptor activity / calmodulin binding / positive regulation of apoptotic process / membrane raft / apical plasma membrane / focal adhesion / negative regulation of apoptotic process / perinuclear region of cytoplasm / cell surface / positive regulation of transcription by RNA polymerase II / mitochondrion / extracellular exosome / nucleoplasm / identical protein binding / membrane / plasma membrane / cytoplasm 類似検索 - 分子機能 | ||||||
生物種 | ![]() | ||||||
手法 | 溶液NMR / simulated annealing | ||||||
![]() | Slepkov, E.R. / Rainey, J.K. / Li, X. / Liu, Y. / Lindhout, D.A. / Sykes, B.D. / Fliegel, L. | ||||||
![]() | ![]() タイトル: Structural and functional characterization of transmembrane segment IV of the NHE1 isoform of the Na+/H+ exchanger. 著者: Slepkov, E.R. / Rainey, J.K. / Li, X. / Liu, Y. / Cheng, F.J. / Lindhout, D.A. / Sykes, B.D. / Fliegel, L. #1: ![]() タイトル: High-yield expression of isotopically labeled peptides for use in NMR studies 著者: Lindhout, D.A. / Thiessen, A. / Schieve, D. / Sykes, B.D. | ||||||
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 | ![]() | 879.3 KB | 表示 | ![]() |
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-検証レポート
文書・要旨 | ![]() | 349.7 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 839.2 KB | 表示 | |
XML形式データ | ![]() | 59.4 KB | 表示 | |
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-関連構造データ
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リンク
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集合体
登録構造単位 | ![]()
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NMR アンサンブル |
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要素
#1: タンパク質・ペプチド | 分子量: 3139.748 Da / 分子数: 1 / 断片: Transmembrane segment IV / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() |
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-実験情報
-実験
実験 | 手法: 溶液NMR | ||||||||||||||||||||
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NMR実験 |
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NMR実験の詳細 | Text: This structure was determined using standard 2D homonuclear techniques with the exception that HNHA J-coupling constants were incorporated. |
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試料調製
詳細 |
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試料状態 | 圧: ambient / 温度: 303 K |
-NMR測定
放射 | プロトコル: SINGLE WAVELENGTH / 単色(M)・ラウエ(L): M | ||||||||||||||||||||
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放射波長 | 相対比: 1 | ||||||||||||||||||||
NMRスペクトロメーター |
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解析
NMR software |
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精密化 | 手法: simulated annealing / ソフトェア番号: 1 詳細: 15 rounds of simulated annealing were carried out to optimize included NOE contacts and lengths, as well as J-HNHA. Finally, homoserine lactone was included. The ensemble of structures given ...詳細: 15 rounds of simulated annealing were carried out to optimize included NOE contacts and lengths, as well as J-HNHA. Finally, homoserine lactone was included. The ensemble of structures given is superposed over the region I169-F176. Other useful superpositions that should be examined are D159-L163 and L165-P168. | ||||||||||||||||||||||||
NMRアンサンブル | コンフォーマー選択の基準: structures with the lowest energy 計算したコンフォーマーの数: 1000 / 登録したコンフォーマーの数: 100 |