+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 1mw4 | ||||||
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タイトル | Solution structure of the human Grb7-SH2 domain in complex with a 10 amino acid peptide pY1139 | ||||||
要素 |
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キーワード | HORMONE/GROWTH FACTOR/TRANSFERASE / SH2 domain in complex with a ligand / HORMONE-GROWTH FACTOR-TRANSFERASE COMPLEX | ||||||
機能・相同性 | 機能・相同性情報 negative regulation of immature T cell proliferation in thymus / ERBB3:ERBB2 complex / ERBB2-ERBB4 signaling pathway / GRB7 events in ERBB2 signaling / immature T cell proliferation in thymus / RNA polymerase I core binding / semaphorin receptor complex / ErbB-3 class receptor binding / regulation of microtubule-based process / Sema4D induced cell migration and growth-cone collapse ...negative regulation of immature T cell proliferation in thymus / ERBB3:ERBB2 complex / ERBB2-ERBB4 signaling pathway / GRB7 events in ERBB2 signaling / immature T cell proliferation in thymus / RNA polymerase I core binding / semaphorin receptor complex / ErbB-3 class receptor binding / regulation of microtubule-based process / Sema4D induced cell migration and growth-cone collapse / motor neuron axon guidance / RND1 GTPase cycle / PLCG1 events in ERBB2 signaling / neurotransmitter receptor localization to postsynaptic specialization membrane / ERBB2-EGFR signaling pathway / positive regulation of Rho protein signal transduction / ERBB2 Activates PTK6 Signaling / neuromuscular junction development / positive regulation of transcription by RNA polymerase I / Drug-mediated inhibition of ERBB2 signaling / Resistance of ERBB2 KD mutants to trastuzumab / Resistance of ERBB2 KD mutants to sapitinib / Resistance of ERBB2 KD mutants to tesevatinib / Resistance of ERBB2 KD mutants to neratinib / Resistance of ERBB2 KD mutants to osimertinib / Resistance of ERBB2 KD mutants to afatinib / Resistance of ERBB2 KD mutants to AEE788 / Resistance of ERBB2 KD mutants to lapatinib / Drug resistance in ERBB2 TMD/JMD mutants / enzyme-linked receptor protein signaling pathway / ERBB2-ERBB3 signaling pathway / oligodendrocyte differentiation / ERBB2 Regulates Cell Motility / semaphorin-plexin signaling pathway / PI3K events in ERBB2 signaling / RET signaling / positive regulation of protein targeting to membrane / regulation of angiogenesis / coreceptor activity / Schwann cell development / cell surface receptor protein tyrosine kinase signaling pathway / stress granule assembly / Signaling by ERBB2 / Tie2 Signaling / cellular response to epidermal growth factor stimulus / TFAP2 (AP-2) family regulates transcription of growth factors and their receptors / myelination / GRB2 events in ERBB2 signaling / transmembrane receptor protein tyrosine kinase activity / phosphatidylinositol 3-kinase/protein kinase B signal transduction / regulation of ERK1 and ERK2 cascade / SHC1 events in ERBB2 signaling / positive regulation of cell adhesion / Downstream signal transduction / Downregulation of ERBB2:ERBB3 signaling / Constitutive Signaling by Overexpressed ERBB2 / neurogenesis / phosphatidylinositol binding / positive regulation of epithelial cell proliferation / basal plasma membrane / cell projection / positive regulation of translation / Signaling by ERBB2 TMD/JMD mutants / positive regulation of MAP kinase activity / wound healing / Signaling by ERBB2 ECD mutants / epidermal growth factor receptor signaling pathway / neuromuscular junction / Signaling by ERBB2 KD Mutants / Signaling by SCF-KIT / receptor protein-tyrosine kinase / neuron differentiation / cellular response to growth factor stimulus / receptor tyrosine kinase binding / Downregulation of ERBB2 signaling / peptidyl-tyrosine phosphorylation / ruffle membrane / cytoplasmic stress granule / Constitutive Signaling by Aberrant PI3K in Cancer / transmembrane signaling receptor activity / PIP3 activates AKT signaling / myelin sheath / heart development / presynaptic membrane / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / RAF/MAP kinase cascade / positive regulation of cell growth / protein tyrosine kinase activity / basolateral plasma membrane / positive regulation of MAPK cascade / negative regulation of translation / early endosome / receptor complex / cell surface receptor signaling pathway / endosome membrane / intracellular signal transduction / positive regulation of cell migration / protein heterodimerization activity / positive regulation of protein phosphorylation / protein phosphorylation 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 | Ivancic, M. / Lyons, B.A. | ||||||
引用 | ジャーナル: J.BIOMOL.NMR / 年: 2003 タイトル: Solution structure of the human Grb7-SH2 domain/erbB2 peptide complex and structural basis for Grb7 binding to ErbB2 著者: Ivancic, M. / Daly, R.J. / Lyons, B.A. #1: ジャーナル: J.Biomol.NMR / 年: 2002 タイトル: Assignment of Backbone 1H, 13C, and 15N Resonances of Human Grb7-SH2 Domain in Complex with a Phosphorylated Peptide Ligand 著者: Brescia, P.J. / Ivancic, M. / Lyons, B.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 | 1mw4.cif.gz | 414.6 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb1mw4.ent.gz | 337.7 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 1mw4.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 | 1mw4_validation.pdf.gz | 367.7 KB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 1mw4_full_validation.pdf.gz | 549.6 KB | 表示 | |
XML形式データ | 1mw4_validation.xml.gz | 55.5 KB | 表示 | |
CIF形式データ | 1mw4_validation.cif.gz | 69.3 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/mw/1mw4 ftp://data.pdbj.org/pub/pdb/validation_reports/mw/1mw4 | HTTPS FTP |
-関連構造データ
類似構造データ | |
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その他のデータベース |
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-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: 13690.711 Da / 分子数: 1 / 断片: SH2 domain / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / プラスミド: pGEX2T / 発現宿主: Escherichia coli (大腸菌) / 株 (発現宿主): BL21 (DE3) PlysS / 参照: UniProt: Q14451 |
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#2: タンパク質・ペプチド | 分子量: 1266.205 Da / 分子数: 1 / 断片: SH2 domain binding site / 由来タイプ: 合成 詳細: The peptide was chemically synthesized. The sequence of the peptide is naturally found in Homo sapiens (human). 参照: UniProt: P04626, receptor protein-tyrosine kinase |
Has protein modification | Y |
-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 using triple-resonance NMR spectroscopy. |
-試料調製
詳細 | 内容: 0.7mM Grb7 SH2 U-15N, 13C, 50mM acetate / 溶媒系: 90% H2O/10% D2O |
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試料状態 | イオン強度: 100 mM NaCl / pH: 6.6 / 圧: 1 atm / 温度: 298 K |
結晶化 | *PLUS 手法: other / 詳細: NMR |
-NMR測定
放射 | プロトコル: SINGLE WAVELENGTH / 単色(M)・ラウエ(L): M / 散乱光タイプ: x-ray |
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放射波長 | 相対比: 1 |
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: 500 MHz |
-解析
NMR software |
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精密化 | 手法: torsion angle dynamics / ソフトェア番号: 1 詳細: THE STRUCTURE IS BASED ON A TOTAL OF 1904 RESTRAINTS: 1660 ARE NOE DERIVED, 120 ARE DIHEDRAL RESTRAINTS AND 124 ARE DISTANCE RESTRAINTS FROM HYDROGEN BONDS. | ||||||||||||||||||||
代表構造 | 選択基準: closest to the average | ||||||||||||||||||||
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: 50 / 登録したコンフォーマーの数: 10 |