+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 1pic | ||||||
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タイトル | PHOSPHATIDYLINOSITOL 3-KINASE, P85-ALPHA SUBUNIT: C-TERMINAL SH2 DOMAIN COMPLEXED WITH A TYR751 PHOSPHOPEPTIDE FROM THE PDGF RECEPTOR, NMR, MINIMIZED MEAN STRUCTURE | ||||||
要素 |
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キーワード | COMPLEX (PHOSPHOTRANSFERASE/RECEPTOR) / PHOSPHOTRANSFERASE / SH2 DOMAIN / SIGNAL TRANSDUCTION / PHOSPHOINOSITIDE 3-KINASE / COMPLEX (PHOSPHOTRANSFERASE-RECEPTOR) / COMPLEX (PHOSPHOTRANSFERASE-RECEPTOR) complex | ||||||
機能・相同性 | 機能・相同性情報 perinuclear endoplasmic reticulum membrane / regulation of toll-like receptor 4 signaling pathway / phosphatidylinositol kinase activity / phosphatidylinositol 3-kinase regulator activity / IRS-mediated signalling / positive regulation of focal adhesion disassembly / phosphatidylinositol 3-kinase activator activity / interleukin-18-mediated signaling pathway / PI3K events in ERBB4 signaling / myeloid leukocyte migration ...perinuclear endoplasmic reticulum membrane / regulation of toll-like receptor 4 signaling pathway / phosphatidylinositol kinase activity / phosphatidylinositol 3-kinase regulator activity / IRS-mediated signalling / positive regulation of focal adhesion disassembly / phosphatidylinositol 3-kinase activator activity / interleukin-18-mediated signaling pathway / PI3K events in ERBB4 signaling / myeloid leukocyte migration / 1-phosphatidylinositol-3-kinase regulator activity / phosphatidylinositol 3-kinase regulatory subunit binding / neurotrophin TRKA receptor binding / Activated NTRK2 signals through PI3K / positive regulation of endoplasmic reticulum unfolded protein response / Activated NTRK3 signals through PI3K / cis-Golgi network / ErbB-3 class receptor binding / kinase activator activity / transmembrane receptor protein tyrosine kinase adaptor activity / RHOF GTPase cycle / Signaling by cytosolic FGFR1 fusion mutants / RHOD GTPase cycle / phosphatidylinositol 3-kinase complex, class IA / phosphatidylinositol 3-kinase complex / enzyme-substrate adaptor activity / Nephrin family interactions / Signaling by LTK in cancer / Costimulation by the CD28 family / RND1 GTPase cycle / Signaling by LTK / MET activates PI3K/AKT signaling / positive regulation of leukocyte migration / PI3K/AKT activation / RND2 GTPase cycle / positive regulation of filopodium assembly / RND3 GTPase cycle / growth hormone receptor signaling pathway / negative regulation of stress fiber assembly / insulin binding / natural killer cell mediated cytotoxicity / RHOV GTPase cycle / negative regulation of cell-matrix adhesion / Signaling by ALK / RHOB GTPase cycle / GP1b-IX-V activation signalling / PI-3K cascade:FGFR2 / PI-3K cascade:FGFR3 / Erythropoietin activates Phosphoinositide-3-kinase (PI3K) / PI-3K cascade:FGFR4 / PI-3K cascade:FGFR1 / RHOC GTPase cycle / RHOJ GTPase cycle / negative regulation of osteoclast differentiation / intracellular glucose homeostasis / Synthesis of PIPs at the plasma membrane / phosphatidylinositol phosphate biosynthetic process / CD28 dependent PI3K/Akt signaling / RHOU GTPase cycle / CDC42 GTPase cycle / PI3K events in ERBB2 signaling / PI3K Cascade / RET signaling / insulin receptor substrate binding / Interleukin-3, Interleukin-5 and GM-CSF signaling / T cell differentiation / RHOG GTPase cycle / extrinsic apoptotic signaling pathway via death domain receptors / RHOA GTPase cycle / RAC2 GTPase cycle / RAC3 GTPase cycle / GAB1 signalosome / Role of LAT2/NTAL/LAB on calcium mobilization / Role of phospholipids in phagocytosis / Interleukin receptor SHC signaling / phosphatidylinositol 3-kinase binding / positive regulation of lamellipodium assembly / Signaling by PDGFRA transmembrane, juxtamembrane and kinase domain mutants / Signaling by PDGFRA extracellular domain mutants / Signaling by FGFR4 in disease / Signaling by FLT3 ITD and TKD mutants / Signaling by FGFR2 in disease / Signaling by FGFR3 in disease / GPVI-mediated activation cascade / Tie2 Signaling / insulin-like growth factor receptor binding / FLT3 Signaling / Signaling by FLT3 fusion proteins / phosphotyrosine residue binding / RAC1 GTPase cycle / response to endoplasmic reticulum stress / Signaling by FGFR1 in disease / Interleukin-7 signaling / phosphatidylinositol 3-kinase/protein kinase B signal transduction / Downstream signal transduction / substrate adhesion-dependent cell spreading / B cell differentiation / osteoclast differentiation / positive regulation of RNA splicing / insulin-like growth factor receptor signaling pathway 類似検索 - 分子機能 | ||||||
生物種 | Homo sapiens (ヒト) | ||||||
手法 | 溶液NMR / simulated annealing | ||||||
データ登録者 | Breeze, A.L. / Kara, B.V. / Barratt, D.G. / Anderson, M. / Smith, J.C. / Luke, R.W. / Best, J.R. / Cartlidge, S.A. | ||||||
引用 | ジャーナル: EMBO J. / 年: 1996 タイトル: Structure of a specific peptide complex of the carboxy-terminal SH2 domain from the p85 alpha subunit of phosphatidylinositol 3-kinase. 著者: Breeze, A.L. / Kara, B.V. / Barratt, D.G. / Anderson, M. / Smith, J.C. / Luke, R.W. / Best, J.R. / Cartlidge, S.A. | ||||||
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 | 1pic.cif.gz | 53.3 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb1pic.ent.gz | 38.5 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 1pic.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 | 1pic_validation.pdf.gz | 259 KB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 1pic_full_validation.pdf.gz | 258.8 KB | 表示 | |
XML形式データ | 1pic_validation.xml.gz | 5.6 KB | 表示 | |
CIF形式データ | 1pic_validation.cif.gz | 7 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/pi/1pic ftp://data.pdbj.org/pub/pdb/validation_reports/pi/1pic | 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: 12612.094 Da / 分子数: 1 断片: C-TERMINAL SH2 DOMAIN, RESIDUES 617 - 724 OF P85-ALPHA REGULATORY SUBUNIT 由来タイプ: 組換発現 詳細: CONTAINS AN N-TERMINAL EXTENSION (GSPI) DERIVED FROM THE RECOMBINANT EXPRESSION VECTOR 由来: (組換発現) Homo sapiens (ヒト) / 発現宿主: Escherichia coli (大腸菌) / 株 (発現宿主): W3110 (CGSC 6564) / 参照: UniProt: P27986, phosphatidylinositol 3-kinase |
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#2: タンパク質・ペプチド | 分子量: 727.805 Da / 分子数: 1 / 断片: ACETYL-PTYR-VAL-PRO-MET-LEU, RESIDUES 751 - 755 / 由来タイプ: 組換発現 詳細: TYROSINE-PHOSPHORYLATED PEPTIDE INCORPORATES AN N-TERMINAL ACETYL GROUP |
Has protein modification | Y |
-実験情報
-実験
実験 | 手法: 溶液NMR |
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NMR実験の詳細 | Text: THE STRUCTURE WAS DETERMINED BY TRIPLE-RESONANCE NMR ON 13C,15N-LABELLED SH2 DOMAIN COMBINED WITH ISOTOPE-FILTERED 1H-NMR FOR THE UNLABELLED BOUND PEPTIDE. |
-試料調製
試料状態 | pH: 6.8 / 温度: 296 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 |
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-解析
ソフトウェア |
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NMR software |
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精密化 | 手法: simulated annealing / ソフトェア番号: 1 詳細: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE. | ||||||||||||
NMRアンサンブル | 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: 1 |