+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 1fu5 | ||||||
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タイトル | NMR STRUCTURE OF THE N-SH2 DOMAIN OF THE P85 SUBUNIT OF PI3-KINASE COMPLEXED TO A DOUBLY PHOSPHORYLATED PEPTIDE DERIVED FROM POLYOMAVIRUS MIDDLE T ANTIGEN | ||||||
要素 |
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キーワード | PEPTIDE BINDING PROTEIN / protein-peptide complex | ||||||
機能・相同性 | 機能・相同性情報 PI3K events in ERBB4 signaling / Costimulation by the CD28 family / CD28 dependent PI3K/Akt signaling / MET activates PI3K/AKT signaling / Erythropoietin activates Phosphoinositide-3-kinase (PI3K) / Interleukin receptor SHC signaling / Tie2 Signaling / Interleukin-3, Interleukin-5 and GM-CSF signaling / FLT3 Signaling / GAB1 signalosome ...PI3K events in ERBB4 signaling / Costimulation by the CD28 family / CD28 dependent PI3K/Akt signaling / MET activates PI3K/AKT signaling / Erythropoietin activates Phosphoinositide-3-kinase (PI3K) / Interleukin receptor SHC signaling / Tie2 Signaling / Interleukin-3, Interleukin-5 and GM-CSF signaling / FLT3 Signaling / GAB1 signalosome / PI3K events in ERBB2 signaling / PI-3K cascade:FGFR1 / PI-3K cascade:FGFR3 / PI-3K cascade:FGFR4 / RHOJ GTPase cycle / RND2 GTPase cycle / RND1 GTPase cycle / IRS-mediated signalling / Interleukin-7 signaling / GP1b-IX-V activation signalling / Signaling by LTK / Synthesis of PIPs at the plasma membrane / PI3K/AKT activation / PI-3K cascade:FGFR2 / Regulation of signaling by CBL / Downstream TCR signaling / RHOF GTPase cycle / PI3K Cascade / VEGFA-VEGFR2 Pathway / Signaling by SCF-KIT / Role of LAT2/NTAL/LAB on calcium mobilization / RHOB GTPase cycle / CDC42 GTPase cycle / RHOD GTPase cycle / RND3 GTPase cycle / GPVI-mediated activation cascade / PIP3 activates AKT signaling / Downstream signal transduction / Signaling by ALK / RHOG GTPase cycle / Role of phospholipids in phagocytosis / RAC2 GTPase cycle / RHOU GTPase cycle / RHOV GTPase cycle / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / DAP12 signaling / RAC1 GTPase cycle / RET signaling / RHOA GTPase cycle / Extra-nuclear estrogen signaling / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / perinuclear endoplasmic reticulum membrane / response to yeast / regulation of toll-like receptor 4 signaling pathway / phosphatidylinositol metabolic process / negative regulation of muscle cell apoptotic process / phosphatidylinositol 3-kinase regulator activity / positive regulation of focal adhesion disassembly / interleukin-18-mediated signaling pathway / response to fatty acid / myeloid leukocyte migration / response to fructose / 1-phosphatidylinositol-3-kinase regulator activity / phosphatidylinositol 3-kinase regulatory subunit binding / neurotrophin TRKA receptor binding / response to growth factor / cis-Golgi network / ErbB-3 class receptor binding / kinase activator activity / negative regulation of cell adhesion / platelet-derived growth factor receptor binding / regulation of stress fiber assembly / positive regulation of endoplasmic reticulum unfolded protein response / G alpha (q) signalling events / phosphatidylinositol 3-kinase complex, class IA / positive regulation of synapse assembly / phosphatidylinositol 3-kinase complex / response to iron(II) ion / RAF/MAP kinase cascade / positive regulation of leukocyte migration / positive regulation of filopodium assembly / negative regulation of stress fiber assembly / growth hormone receptor signaling pathway / cellular response to fatty acid / insulin binding / negative regulation of heart rate / 1-phosphatidylinositol-3-kinase activity / negative regulation of cell-matrix adhesion / negative regulation of cell-cell adhesion / response to testosterone / response to dexamethasone / negative regulation of osteoclast differentiation / intracellular glucose homeostasis / phosphatidylinositol phosphate biosynthetic process / host cell membrane / insulin receptor substrate binding / extrinsic apoptotic signaling pathway via death domain receptors / response to amino acid / regulation of protein localization to plasma membrane / positive regulation of myoblast differentiation 類似検索 - 分子機能 | ||||||
生物種 | Rattus norvegicus (ドブネズミ) | ||||||
手法 | 溶液NMR / The structures were energy minimized with MSI DISCOVER. | ||||||
データ登録者 | Weber, T. / Schaffhausen, B. / Liu, Y. / Guenther, U.L. | ||||||
引用 | ジャーナル: Biochemistry / 年: 2000 タイトル: NMR structure of the N-SH2 of the p85 subunit of phosphoinositide 3-kinase complexed to a doubly phosphorylated peptide reveals a second phosphotyrosine binding site. 著者: Weber, T. / Schaffhausen, B. / Liu, Y. / Gunther, U.L. | ||||||
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 | 1fu5.cif.gz | 49.5 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb1fu5.ent.gz | 39.6 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 1fu5.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 | 1fu5_validation.pdf.gz | 268.3 KB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 1fu5_full_validation.pdf.gz | 268.1 KB | 表示 | |
XML形式データ | 1fu5_validation.xml.gz | 6.6 KB | 表示 | |
CIF形式データ | 1fu5_validation.cif.gz | 8.3 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/fu/1fu5 ftp://data.pdbj.org/pub/pdb/validation_reports/fu/1fu5 | 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: 12870.384 Da / 分子数: 1 断片: RESIDUES 321 TO 431 OF P85, N-SH2 (SRC HOMOLOGY 2) DOMAIN 由来タイプ: 組換発現 / 由来: (組換発現) Rattus norvegicus (ドブネズミ) / 発現宿主: Escherichia coli (大腸菌) / 参照: UniProt: Q63787 |
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#2: タンパク質・ペプチド | 分子量: 2063.089 Da / 分子数: 1 断片: RESIDUES 312 TO 326 OF MT ANTIGEN, Y315 AND Y322 PHOSPHORYLATED 由来タイプ: 合成 詳細: MT peptide was synthesized by the Tufts Protein Chemistry Facility 参照: UniProt: P03076, UniProt: P03077*PLUS |
-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: NOESY assignments were obtained by a semi-automatic procedure employing a program from Pristovsek [Pristovsek, P. & Kidric, J. (1997) Biopol. 42, 671-679)]. Initial calculations included only ...Text: NOESY assignments were obtained by a semi-automatic procedure employing a program from Pristovsek [Pristovsek, P. & Kidric, J. (1997) Biopol. 42, 671-679)]. Initial calculations included only intramolecular constraints. The observed NOEs derived from 13C{F1}-filtered 2D-NOESY spectra were incorporated into the structure calculation when the protein fold was already correct. |
-試料調製
詳細 | 内容: 0.15mM N-SH2 15N, 13C; MT peptide; 0.1mM KCl; 95% H2O, 5% D2O 溶媒系: 100% H2O |
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試料状態 | イオン強度: 0.1mM / pH: 6.8 / 圧: 1 bar / 温度: 305 K |
結晶化 | *PLUS 手法: other / 詳細: NMR |
-NMR測定
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: The structures were energy minimized with MSI DISCOVER. ソフトェア番号: 1 / 詳細: The structure with the lowest energy is presented | ||||||||||||||||||
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 favorable non-bond energy 計算したコンフォーマーの数: 110 / 登録したコンフォーマーの数: 1 |