+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 1oei | ||||||
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タイトル | Human prion protein 61-84 | ||||||
要素 | MAJOR PRION PROTEIN | ||||||
キーワード | PRION PROTEIN / OCTAPEPTIDE REPEATS / PROTEIN AGGREGATION / PH-DEPENDENT CONFORMATION / BRAIN / DISEASE MUTATION | ||||||
機能・相同性 | 機能・相同性情報 positive regulation of glutamate receptor signaling pathway / negative regulation of amyloid precursor protein catabolic process / lamin binding / regulation of glutamate receptor signaling pathway / regulation of calcium ion import across plasma membrane / aspartic-type endopeptidase inhibitor activity / glycosaminoglycan binding / ATP-dependent protein binding / regulation of potassium ion transmembrane transport / negative regulation of interleukin-17 production ...positive regulation of glutamate receptor signaling pathway / negative regulation of amyloid precursor protein catabolic process / lamin binding / regulation of glutamate receptor signaling pathway / regulation of calcium ion import across plasma membrane / aspartic-type endopeptidase inhibitor activity / glycosaminoglycan binding / ATP-dependent protein binding / regulation of potassium ion transmembrane transport / negative regulation of interleukin-17 production / NCAM1 interactions / negative regulation of dendritic spine maintenance / type 5 metabotropic glutamate receptor binding / cupric ion binding / negative regulation of protein processing / negative regulation of calcineurin-NFAT signaling cascade / dendritic spine maintenance / negative regulation of interleukin-2 production / negative regulation of T cell receptor signaling pathway / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / extrinsic component of membrane / cuprous ion binding / negative regulation of amyloid-beta formation / negative regulation of activated T cell proliferation / response to amyloid-beta / : / negative regulation of type II interferon production / negative regulation of long-term synaptic potentiation / intracellular copper ion homeostasis / positive regulation of protein targeting to membrane / long-term memory / response to cadmium ion / regulation of peptidyl-tyrosine phosphorylation / inclusion body / cellular response to copper ion / neuron projection maintenance / tubulin binding / negative regulation of protein phosphorylation / molecular condensate scaffold activity / molecular function activator activity / positive regulation of protein localization to plasma membrane / protein destabilization / protein homooligomerization / negative regulation of DNA-binding transcription factor activity / terminal bouton / cellular response to amyloid-beta / positive regulation of peptidyl-tyrosine phosphorylation / positive regulation of neuron apoptotic process / cellular response to xenobiotic stimulus / signaling receptor activity / amyloid-beta binding / protein-folding chaperone binding / postsynapse / microtubule binding / nuclear membrane / protease binding / response to oxidative stress / transmembrane transporter binding / molecular adaptor activity / postsynaptic density / learning or memory / regulation of cell cycle / membrane raft / cell cycle / copper ion binding / external side of plasma membrane / intracellular membrane-bounded organelle / dendrite / protein-containing complex binding / negative regulation of apoptotic process / Golgi apparatus / cell surface / endoplasmic reticulum / extracellular exosome / identical protein binding / plasma membrane / cytoplasm / cytosol 類似検索 - 分子機能 | ||||||
生物種 | HOMO SAPIENS (ヒト) | ||||||
手法 | 溶液NMR / torsion angle dynamics | ||||||
データ登録者 | Zahn, R. | ||||||
引用 | ジャーナル: J.Mol.Biol. / 年: 2003 タイトル: The Octapeptide Repeats in Mammalian Prion Protein Constitute a Ph-Dependent Folding and Aggregation Site 著者: Zahn, R. | ||||||
履歴 |
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-構造の表示
構造ビューア | 分子: MolmilJmol/JSmol |
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-ダウンロードとリンク
-ダウンロード
PDBx/mmCIF形式 | 1oei.cif.gz | 106.4 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb1oei.ent.gz | 79.1 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 1oei.json.gz | ツリー表示 | PDBx/mmJSON形式 | |
その他 | その他のダウンロード |
-検証レポート
文書・要旨 | 1oei_validation.pdf.gz | 340.3 KB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 1oei_full_validation.pdf.gz | 457.6 KB | 表示 | |
XML形式データ | 1oei_validation.xml.gz | 8.4 KB | 表示 | |
CIF形式データ | 1oei_validation.cif.gz | 14 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/oe/1oei ftp://data.pdbj.org/pub/pdb/validation_reports/oe/1oei | HTTPS FTP |
-関連構造データ
-リンク
-集合体
登録構造単位 |
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1 |
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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: 2351.437 Da / 分子数: 1 / 断片: RESIDUES 61-84 / 由来タイプ: 組換発現 / 由来: (組換発現) HOMO SAPIENS (ヒト) / 器官: BRAIN / プラスミド: PRSET A / 発現宿主: ESCHERICHIA COLI (大腸菌) / 株 (発現宿主): BL21(DE3) / 参照: UniProt: P04156 |
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構成要素の詳細 | THE PHYSIOLOGI |
-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: THE STRUCTURE WAS DETERMINED ON 15N-LABELED PROTEIN |
-試料調製
試料状態 | pH: 4.5 / 圧: 1 atm / 温度: 293 K |
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-NMR測定
NMRスペクトロメーター | タイプ: Bruker DRX / 製造業者: Bruker / モデル: DRX / 磁場強度: 800 MHz |
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-解析
NMR software |
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精密化 | 手法: torsion angle dynamics / ソフトェア番号: 1 | |||||||||
NMRアンサンブル | コンフォーマー選択の基準: LEAST RESTRAINT VIOLATION 計算したコンフォーマーの数: 100 / 登録したコンフォーマーの数: 20 |