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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: 8cte | ||||||
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タイトル | Class 2 of erythrocyte ankyrin-1 complex (Composite map) | ||||||
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![]() | TRANSPORT PROTEIN/STRUCTURAL PROTEIN / Membrane Protein / Anion Exchange / Erythrocyte / Glycoprotein / TRANSPORT PROTEIN-STRUCTURAL PROTEIN complex | ||||||
機能・相同性 | ![]() nitric oxide transmembrane transporter activity / metanephric descending thin limb development / metanephric proximal straight tubule development / metanephric proximal convoluted tubule segment 2 development / metanephric glomerulus vasculature development / cerebrospinal fluid secretion / methylammonium transmembrane transport / Defective RHAG causes regulator type Rh-null hemolytic anemia (RHN) / Rhesus blood group biosynthesis / methylammonium transmembrane transporter activity ...nitric oxide transmembrane transporter activity / metanephric descending thin limb development / metanephric proximal straight tubule development / metanephric proximal convoluted tubule segment 2 development / metanephric glomerulus vasculature development / cerebrospinal fluid secretion / methylammonium transmembrane transport / Defective RHAG causes regulator type Rh-null hemolytic anemia (RHN) / Rhesus blood group biosynthesis / methylammonium transmembrane transporter activity / lipid digestion / Rhesus glycoproteins mediate ammonium transport. / cellular response to salt stress / renal water transport / glycerol transmembrane transporter activity / corticotropin secretion / secretory granule organization / carbon dioxide transmembrane transport / carbon dioxide transmembrane transporter activity / renal water absorption / positive regulation of saliva secretion / Passive transport by Aquaporins / glycerol transmembrane transport / water transmembrane transporter activity / ammonium homeostasis / establishment or maintenance of actin cytoskeleton polarity / pancreatic juice secretion / cellular response to mercury ion / lateral ventricle development / spectrin-associated cytoskeleton / hemoglobin metabolic process / positive regulation of organelle organization / potassium ion transmembrane transporter activity / : / intracellular water homeostasis / protein-glutamine gamma-glutamyltransferase activity / maintenance of epithelial cell apical/basal polarity / ammonium transmembrane transport / leak channel activity / water transport / water channel activity / pH elevation / Defective SLC4A1 causes hereditary spherocytosis type 4 (HSP4), distal renal tubular acidosis (dRTA) and dRTA with hemolytic anemia (dRTA-HA) / negative regulation of urine volume / transepithelial water transport / glomerular filtration / NrCAM interactions / Bicarbonate transporters / Neurofascin interactions / intracellular monoatomic ion homeostasis / ankyrin-1 complex / intracellularly cGMP-activated cation channel activity / plasma membrane phospholipid scrambling / CHL1 interactions / monoatomic anion transmembrane transporter activity / ammonium channel activity / chloride:bicarbonate antiporter activity / camera-type eye morphogenesis / cytoskeletal anchor activity / fibroblast migration / multicellular organismal-level water homeostasis / solute:inorganic anion antiporter activity / cellular homeostasis / cellular hyperosmotic response / hyperosmotic response / renal water homeostasis / bicarbonate transport / cell volume homeostasis / bicarbonate transmembrane transporter activity / M band / positive regulation of fibroblast migration / monoatomic anion transport / Interaction between L1 and Ankyrins / inorganic cation transmembrane transport / chloride transport / odontogenesis / chloride transmembrane transporter activity / nitric oxide transport / ankyrin binding / negative regulation of glycolytic process through fructose-6-phosphate / hemoglobin binding / spectrin binding / cortical cytoskeleton / cGMP-mediated signaling / exocytosis / erythrocyte maturation / potassium channel activity / brush border / transmembrane transporter activity / axolemma / cellular response to nitric oxide / erythrocyte development / endoplasmic reticulum to Golgi vesicle-mediated transport / COPI-mediated anterograde transport / cellular response to retinoic acid / protein-membrane adaptor activity / cellular response to cAMP / spleen development / sensory perception of pain / chloride transmembrane transport 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: 2.9 Å | ||||||
![]() | Vallese, F. / Kim, K. / Yen, L.Y. / Johnston, J.D. / Noble, A.J. / Cali, T. / Clarke, O.B. | ||||||
資金援助 | 1件
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![]() | ![]() タイトル: Architecture of the human erythrocyte ankyrin-1 complex. 著者: Francesca Vallese / Kookjoo Kim / Laura Y Yen / Jake D Johnston / Alex J Noble / Tito Calì / Oliver Biggs Clarke / ![]() ![]() 要旨: The stability and shape of the erythrocyte membrane is provided by the ankyrin-1 complex, but how it tethers the spectrin-actin cytoskeleton to the lipid bilayer and the nature of its association ...The stability and shape of the erythrocyte membrane is provided by the ankyrin-1 complex, but how it tethers the spectrin-actin cytoskeleton to the lipid bilayer and the nature of its association with the band 3 anion exchanger and the Rhesus glycoproteins remains unknown. Here we present structures of ankyrin-1 complexes purified from human erythrocytes. We reveal the architecture of a core complex of ankyrin-1, the Rhesus proteins RhAG and RhCE, the band 3 anion exchanger, protein 4.2, glycophorin A and glycophorin B. The distinct T-shaped conformation of membrane-bound ankyrin-1 facilitates recognition of RhCE and, unexpectedly, the water channel aquaporin-1. Together, our results uncover the molecular details of ankyrin-1 association with the erythrocyte membrane, and illustrate the mechanism of ankyrin-mediated membrane protein clustering. | ||||||
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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ダウンロードとリンク
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PDBx/mmCIF形式 | ![]() | 992.8 KB | 表示 | ![]() |
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PDB形式 | ![]() | 787.2 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 | ![]() | 1.8 MB | 表示 | ![]() |
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文書・詳細版 | ![]() | 1.8 MB | 表示 | |
XML形式データ | ![]() | 137.8 KB | 表示 | |
CIF形式データ | ![]() | 207.9 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 | ![]() 26988MC ![]() 7uz3C ![]() 7uzeC ![]() 7uzqC ![]() 7uzsC ![]() 7uzuC ![]() 7uzvC ![]() 7v07C ![]() 7v0kC ![]() 7v0mC ![]() 7v0qC ![]() 7v0sC ![]() 7v0tC ![]() 7v0uC ![]() 7v0xC ![]() 7v0yC ![]() 7v19C ![]() 8crqC ![]() 8crrC ![]() 8crtC ![]() 8cs9C ![]() 8cslC ![]() 8csvC ![]() 8cswC ![]() 8csxC ![]() 8csyC ![]() 8ct2C ![]() 8ct3C 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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類似構造データ | 類似検索 - 機能・相同性 ![]() |
実験データセット #1 | データ参照: ![]() |
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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
-タンパク質 , 7種, 14分子 AWPTXKLQNDSORM
#1: タンパク質 | 分子量: 206522.625 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) ![]() | ||||||||||
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#2: タンパク質 | 分子量: 101883.859 Da / 分子数: 3 / 由来タイプ: 天然 / 由来: (天然) ![]() #3: タンパク質 | | 分子量: 77096.914 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) ![]() #4: タンパク質 | | 分子量: 45598.918 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) ![]() #5: タンパク質 | 分子量: 44229.629 Da / 分子数: 2 / 由来タイプ: 天然 / 由来: (天然) ![]() #6: タンパク質 | 分子量: 16348.433 Da / 分子数: 2 / 由来タイプ: 天然 / 由来: (天然) ![]() #7: タンパク質 | 分子量: 28788.320 Da / 分子数: 4 / 由来タイプ: 天然 / 由来: (天然) ![]() |
-糖 , 1種, 2分子 ![](data/chem/img/NAG.gif)
#10: 糖 |
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-非ポリマー , 3種, 14分子 ![](data/chem/img/CLR.gif)
![](data/chem/img/AJP.gif)
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#8: 化合物 | ChemComp-CLR / #9: 化合物 | #11: 化合物 | |
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-詳細
研究の焦点であるリガンドがあるか | 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: Class 1 of erythrocyte ankyrin complex (composite map) タイプ: COMPLEX / Entity ID: #1-#7 / 由来: NATURAL |
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由来(天然) | 生物種: ![]() |
緩衝液 | pH: 7.4 詳細: Final gel filtration buffer contained 0.05% w/v digitonin, 130 mM KCl, 20 mM HEPES, pH 7.4, 1 mM ATP, 1 mM MgCl2, 1 mM PMSF. Peak fractions were concentrated to 8 mg/mL, and 0.01% w/v ...詳細: Final gel filtration buffer contained 0.05% w/v digitonin, 130 mM KCl, 20 mM HEPES, pH 7.4, 1 mM ATP, 1 mM MgCl2, 1 mM PMSF. Peak fractions were concentrated to 8 mg/mL, and 0.01% w/v glycyrrhizic acid was added immediately prior to vitrification. |
試料 | 濃度: 8 mg/ml / 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES 詳細: Ankyrin complex mixture purified from digitonin-solubilized erythrocyte ghost membranes |
急速凍結 | 装置: FEI VITROBOT MARK IV / 凍結剤: ETHANE / 湿度: 100 % / 凍結前の試料温度: 277 K / 詳細: 4-6 seconds, wait time 30 seconds |
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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 / 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 / Cs: 2.7 mm / アライメント法: COMA FREE |
試料ホルダ | 凍結剤: NITROGEN 試料ホルダーモデル: FEI TITAN KRIOS AUTOGRID HOLDER |
撮影 | 平均露光時間: 2.5 sec. / 電子線照射量: 58 e/Å2 / フィルム・検出器のモデル: GATAN K3 (6k x 4k) / 撮影したグリッド数: 2 / 実像数: 14464 / 詳細: Two grids were imaged in a single session. |
電子光学装置 | エネルギーフィルター名称: GIF Bioquantum / エネルギーフィルタースリット幅: 20 eV |
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解析
ソフトウェア | 名称: PHENIX / バージョン: 1.20.1_4487: / 分類: 精密化 | ||||||||||||||||||||||||
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EMソフトウェア |
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CTF補正 | 詳細: Patch CTF (cryoSPARC v3) followed by per particle defocus refinement and refinement of higher order aberrations (cryoSPARC v3) タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3次元再構成 | 解像度: 2.9 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 145465 詳細: Composite reconstruction; local refinements aligned to global consensus refinement, provided in additional maps. 対称性のタイプ: POINT | ||||||||||||||||||||||||
拘束条件 |
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