+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 1hjn | ||||||
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タイトル | HUMAN PRION PROTEIN AT PH 7.0 | ||||||
要素 | MAJOR PRION PROTEIN PRECURSOR | ||||||
キーワード | PRION PROTEIN / PRION / BRAIN / GLYCOPROTEIN / GPI-ANCHOR | ||||||
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 | Calzolai, L. / Zahn, R. | ||||||
引用 | ジャーナル: J.Biol.Chem. / 年: 2003 タイトル: Influence of Ph on NMR Structure and Stability of the Human Prion Protein Globular Domain 著者: Calzolai, L. / 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 | 1hjn.cif.gz | 649.4 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb1hjn.ent.gz | 546.8 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 1hjn.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 | 1hjn_validation.pdf.gz | 355.8 KB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 1hjn_full_validation.pdf.gz | 472 KB | 表示 | |
XML形式データ | 1hjn_validation.xml.gz | 29.9 KB | 表示 | |
CIF形式データ | 1hjn_validation.cif.gz | 53.4 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/hj/1hjn ftp://data.pdbj.org/pub/pdb/validation_reports/hj/1hjn | 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 | 分子量: 12559.972 Da / 分子数: 1 / 断片: GLOBULAR DOMAIN, RESIDUES 125-228 / 由来タイプ: 組換発現 / 由来: (組換発現) HOMO SAPIENS (ヒト) / 発現宿主: ESCHERICHIA COLI (大腸菌) / 参照: UniProt: P04156 |
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-実験情報
-実験
実験 | 手法: 溶液NMR |
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-試料調製
試料状態 | pH: 7.0 / 温度: 293 K |
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結晶化 | *PLUS 手法: other / 詳細: NMR |
-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: 750 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: LOWER TARGET FUNCTION / 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: 20 |