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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: 2ko2 | ||||||
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タイトル | NOGO66 | ||||||
![]() | Reticulon-4 | ||||||
![]() | MEMBRANE PROTEIN / NOGO / peripheral / DPC micelle / myelin inhibitor / Endoplasmic reticulum / Membrane / Phosphoprotein / Transmembrane | ||||||
機能・相同性 | ![]() cell adhesion involved in sprouting angiogenesis / positive regulation of ERBB3 signaling pathway / endoplasmic reticulum tubular network formation / endoplasmic reticulum tubular network organization / cerebral cortex radial glia-guided migration / regulation of nervous system development / positive regulation of neutrophil migration / negative regulation of neuron projection regeneration / endoplasmic reticulum tubular network membrane organization / Axonal growth inhibition (RHOA activation) ...cell adhesion involved in sprouting angiogenesis / positive regulation of ERBB3 signaling pathway / endoplasmic reticulum tubular network formation / endoplasmic reticulum tubular network organization / cerebral cortex radial glia-guided migration / regulation of nervous system development / positive regulation of neutrophil migration / negative regulation of neuron projection regeneration / endoplasmic reticulum tubular network membrane organization / Axonal growth inhibition (RHOA activation) / endoplasmic reticulum tubular network membrane / negative regulation of vasculogenesis / : / positive regulation of artery morphogenesis / positive regulation of glial cell differentiation / positive regulation of macrophage migration / : / cell migration involved in vasculogenesis / positive regulation of protein localization to endoplasmic reticulum / intracellular sphingolipid homeostasis / endoplasmic reticulum tubular network / regulation of branching morphogenesis of a nerve / central nervous system vasculogenesis / positive regulation of toll-like receptor 9 signaling pathway / positive regulation of mammary gland epithelial cell proliferation / negative regulation of axonogenesis / nuclear pore complex assembly / regulation of sensory perception of pain / protein localization to lysosome / cardiac epithelial to mesenchymal transition / negative regulation of axon extension / positive regulation of dopamine secretion / leukocyte migration involved in inflammatory response / blastocyst formation / endoplasmic reticulum organization / positive regulation of hepatocyte proliferation / axonal fasciculation / positive regulation of macrophage cytokine production / positive regulation of epithelial cell migration / positive regulation of Rac protein signal transduction / negative regulation of amyloid-beta formation / negative regulation of neuron differentiation / regulation of cell migration / cell projection / negative regulation of cell growth / positive regulation of angiogenesis / nuclear envelope / cell junction / negative regulation of neuron projection development / myelin sheath / cellular response to hypoxia / nervous system development / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / postsynaptic density / protein stabilization / cadherin binding / neuron projection / neuronal cell body / ubiquitin protein ligase binding / glutamatergic synapse / endoplasmic reticulum membrane / protein-containing complex binding / endoplasmic reticulum / protein homodimerization activity / protein-containing complex / plasma membrane / cytoplasm 類似検索 - 分子機能 | ||||||
生物種 | ![]() ![]() | ||||||
手法 | 溶液NMR / simulated annealing | ||||||
Model details | lowest energy, model 1 | ||||||
![]() | Cocco, M.J. / Schulz, J. / Vasudevan, S.V. | ||||||
![]() | ![]() タイトル: Protein folding at the membrane interface, the structure of Nogo-66 requires interactions with a phosphocholine surface. 著者: Vasudevan, S.V. / Schulz, J. / Zhou, C. / Cocco, M.J. | ||||||
履歴 |
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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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ダウンロード
PDBx/mmCIF形式 | ![]() | 218.1 KB | 表示 | ![]() |
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PDB形式 | ![]() | 179.6 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 | ![]() | 343.4 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 423.2 KB | 表示 | |
XML形式データ | ![]() | 15.5 KB | 表示 | |
CIF形式データ | ![]() | 23.6 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-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 | 分子量: 9144.463 Da / 分子数: 1 / 断片: Extracellular domain (UNP residues 1025-1090) / 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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試料調製
詳細 |
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試料 |
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試料状態 | イオン強度: 0 / pH: 4 / 圧: AMBIENT / 温度: 308 K |
-NMR測定
NMRスペクトロメーター | タイプ: VARIAN INOVA / 製造業者: Varian / モデル: INOVA / 磁場強度: 800 MHz |
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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: XPLOR-NIH WAS USED FOR REFINING THE FOLDED PROTEINS. DIHERAL ANGLE RESTRAINTS AND PRE RESTRAINTS WERE ADDED DURING REFINEMENT. | ||||||||||||||||||||
代表構造 | 選択基準: lowest energy | ||||||||||||||||||||
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: 20 / 登録したコンフォーマーの数: 10 |