+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 1ju5 | ||||||
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タイトル | Ternary complex of an Crk SH2 domain, Crk-derived phophopeptide, and Abl SH3 domain by NMR spectroscopy | ||||||
要素 |
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キーワード | PROTEIN BINDING/TRANSFERASE / Crk / SH2 / Abl / SH3 / adaptor protein / phosphopeptide / PROTEIN BINDING-TRANSFERASE COMPLEX | ||||||
機能・相同性 | 機能・相同性情報 PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases / ARMS-mediated activation / MET activates RAP1 and RAC1 / MET receptor recycling / response to hepatocyte growth factor / cellular response to endothelin / helper T cell diapedesis / cerebellar neuron development / response to cholecystokinin / regulation of leukocyte migration ...PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases / ARMS-mediated activation / MET activates RAP1 and RAC1 / MET receptor recycling / response to hepatocyte growth factor / cellular response to endothelin / helper T cell diapedesis / cerebellar neuron development / response to cholecystokinin / regulation of leukocyte migration / response to peptide / Downstream signal transduction / regulation of intracellular signal transduction / postsynaptic specialization assembly / protein phosphorylated amino acid binding / regulation of T cell migration / p130Cas linkage to MAPK signaling for integrins / reelin-mediated signaling pathway / negative regulation of phospholipase C activity / positive regulation of actin filament binding / regulation of dendrite development / positive regulation of oxidoreductase activity / transitional one stage B cell differentiation / protein localization to cytoplasmic microtubule plus-end / DNA conformation change / podocyte apoptotic process / DN4 thymocyte differentiation / Role of ABL in ROBO-SLIT signaling / response to epinephrine / positive regulation of skeletal muscle acetylcholine-gated channel clustering / activation of protein kinase C activity / response to yeast / nicotinate-nucleotide adenylyltransferase activity / Regulation of signaling by CBL / regulation of modification of synaptic structure / regulation of Rac protein signal transduction / positive regulation of extracellular matrix organization / positive regulation of microtubule binding / delta-catenin binding / B cell proliferation involved in immune response / Regulation of actin dynamics for phagocytic cup formation / neuroepithelial cell differentiation / negative regulation of wound healing / microspike assembly / positive regulation of Wnt signaling pathway, planar cell polarity pathway / cerebellum morphogenesis / positive regulation of blood vessel branching / B-1 B cell homeostasis / mitochondrial depolarization / regulation of protein binding / negative regulation of ubiquitin-protein transferase activity / neuropilin signaling pathway / negative regulation of cell motility / neuropilin binding / bubble DNA binding / regulation of Cdc42 protein signal transduction / negative regulation of protein serine/threonine kinase activity / ARMS-mediated activation / activated T cell proliferation / cellular response to dopamine / VEGFA-VEGFR2 Pathway / MET receptor recycling / protein localization to membrane / regulation of cell motility / regulation of axon extension / proline-rich region binding / positive regulation of dendrite development / MET activates RAP1 and RAC1 / mitogen-activated protein kinase binding / myoblast proliferation / alpha-beta T cell differentiation / regulation of hematopoietic stem cell differentiation / cellular response to insulin-like growth factor stimulus / syntaxin binding / negative regulation of natural killer cell mediated cytotoxicity / cardiac muscle cell proliferation / HDR through Single Strand Annealing (SSA) / regulation of T cell differentiation / negative regulation of double-strand break repair via homologous recombination / establishment of cell polarity / positive regulation of cell migration involved in sprouting angiogenesis / regulation of GTPase activity / enzyme-linked receptor protein signaling pathway / Fc-gamma receptor signaling pathway involved in phagocytosis / p130Cas linkage to MAPK signaling for integrins / negative regulation of cell-cell adhesion / Myogenesis / dendrite development / regulation of microtubule polymerization / positive regulation of smooth muscle cell migration / positive regulation of osteoblast proliferation / RUNX2 regulates osteoblast differentiation / positive regulation of Rac protein signal transduction / platelet-derived growth factor receptor-beta signaling pathway / positive regulation of focal adhesion assembly / negative regulation of cellular senescence / negative regulation of long-term synaptic potentiation / regulation of cell adhesion mediated by integrin / Bergmann glial cell differentiation / 学習 類似検索 - 分子機能 | ||||||
生物種 | Homo sapiens (ヒト) Mus musculus (ハツカネズミ) | ||||||
手法 | 溶液NMR / ARIA 1.0, CNS 1.0 | ||||||
データ登録者 | Donaldson, L.W. / Pawson, T. / Kay, L.E. / Forman-Kay, J.D. | ||||||
引用 | ジャーナル: Proc.Natl.Acad.Sci.USA / 年: 2002 タイトル: Structure of a regulatory complex involving the Abl SH3 domain, the Crk SH2 domain, and a Crk-derived phosphopeptide 著者: Donaldson, L.W. / Gish, G. / Pawson, T. / Kay, L.E. / Forman-Kay, J.D. | ||||||
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 | 1ju5.cif.gz | 64.6 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb1ju5.ent.gz | 51.6 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 1ju5.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
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/ju/1ju5 ftp://data.pdbj.org/pub/pdb/validation_reports/ju/1ju5 | HTTPS FTP |
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-関連構造データ
関連構造データ | |
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類似構造データ |
-リンク
-集合体
登録構造単位 |
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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: 12142.571 Da / 分子数: 1 / 断片: Crk 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: pGEX-2T / 生物種 (発現宿主): Escherichia coli / 発現宿主: Escherichia coli BL21 (大腸菌) / 株 (発現宿主): BL21 / 参照: UniProt: P46108 |
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#2: タンパク質・ペプチド | 分子量: 1468.480 Da / 分子数: 1 / 断片: Crk phosphopeptide / 由来タイプ: 組換発現 / 由来: (組換発現) Mus musculus (ハツカネズミ) / プラスミド: pAED4-MMHB / 生物種 (発現宿主): Escherichia coli / 発現宿主: Escherichia coli BL21 (大腸菌) / 株 (発現宿主): BL21 / 参照: UniProt: Q64010 |
#3: タンパク質 | 分子量: 6764.461 Da / 分子数: 1 / 断片: Abl SH3 domain / Mutation: L122K / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / プラスミド: pET15 / 生物種 (発現宿主): Escherichia coli / 発現宿主: Escherichia coli BL21 (大腸菌) / 株 (発現宿主): BL21 / 参照: UniProt: P00519, EC: 2.7.1.112 |
-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: Intermolecular distance restraints were obtained from reverse half-filtered 2D- and 3D-NOESY spectra (300 ms mixing time) on sample in 99% D2O. Methyl prochiral assignments were made on a 10% ...Text: Intermolecular distance restraints were obtained from reverse half-filtered 2D- and 3D-NOESY spectra (300 ms mixing time) on sample in 99% D2O. Methyl prochiral assignments were made on a 10% 13C-labeled sample according to Neri et al (Biochemistry 28:7510; 1989). HACAN and CBCA(CO)N(CA)HA experiments were used to assign the proline residues in the Crk SH2 domain according to Kanelis et al (JBNMR 16:253; 2000) |
-試料調製
詳細 | 内容: 0.6-1.5mM Crk SH2 domain U-15N, 13C; 50mM sodium phosphate pH6.8, 0.02% sodium azide 溶媒系: 90% H2O/10% D2O |
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試料状態 | イオン強度: 50mM sodium phosphate / pH: 6.8 / 圧: ambient / 温度: 303 K |
結晶化 | *PLUS 手法: その他 / 詳細: NMR |
-NMR測定
放射 | プロトコル: SINGLE WAVELENGTH / 単色(M)・ラウエ(L): M | ||||||||||||||||||||
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放射波長 | 相対比: 1 | ||||||||||||||||||||
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: ARIA 1.0, CNS 1.0 / ソフトェア番号: 1 詳細: This structure represents the lowest energy solution based on 2406 SH2 intramolecular restraints, 1628 SH3 intramolecular restraints, 37 SH2-SH3 intermolecular restraints, 64 SH2- ...詳細: This structure represents the lowest energy solution based on 2406 SH2 intramolecular restraints, 1628 SH3 intramolecular restraints, 37 SH2-SH3 intermolecular restraints, 64 SH2-phosphopeptide intermolecular restraints, 50 hydrogen bonds, 54 direct 3J-HNHA couplings and 166 dihedral angle restraints from TALOS Residues 217-220 and 225-229 of the Crk phosphopeptide (Chain B) are disordered. As intermolecular contacts between the SH2 domain (Chain A) and the SH3 domain (Chain C) limited to amino acids 67-75 in DE-loop of the SH2 domain, there is no unique orientation between the SH2 domain and SH3 domain. | ||||||||||||||||||||||||
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 the lowest energy 計算したコンフォーマーの数: 40 / 登録したコンフォーマーの数: 1 |