+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 1bbz | ||||||
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タイトル | CRYSTAL STRUCTURE OF THE ABL-SH3 DOMAIN COMPLEXED WITH A DESIGNED HIGH-AFFINITY PEPTIDE LIGAND: IMPLICATIONS FOR SH3-LIGAND INTERACTIONS | ||||||
要素 |
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キーワード | COMPLEX (TRANSFERASE/PEPTIDE) / COMPLEX (TRANSFERASE-PEPTIDE) / SIGNAL TRANSDUCTION / SH3 DOMAIN / COMPLEX (TRANSFERASE-PEPTIDE) complex | ||||||
機能・相同性 | 機能・相同性情報 : / positive regulation of actin filament binding / positive regulation of oxidoreductase activity / 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 / transitional one stage B cell differentiation ...: / positive regulation of actin filament binding / positive regulation of oxidoreductase activity / 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 / transitional one stage B cell differentiation / activation of protein kinase C activity / nicotinate-nucleotide adenylyltransferase activity / regulation of modification of synaptic structure / positive regulation of microtubule binding / delta-catenin binding / B cell proliferation involved in immune response / positive regulation of extracellular matrix organization / neuroepithelial cell differentiation / 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 / neuropilin signaling pathway / negative regulation of ubiquitin-protein transferase activity / neuropilin binding / bubble DNA binding / negative regulation of protein serine/threonine kinase activity / activated T cell proliferation / cellular response to dopamine / regulation of cell motility / regulation of Cdc42 protein signal transduction / proline-rich region binding / positive regulation of dendrite development / negative regulation of mitotic cell cycle / mitogen-activated protein kinase binding / myoblast proliferation / syntaxin binding / regulation of hematopoietic stem cell differentiation / negative regulation of BMP signaling pathway / alpha-beta T cell differentiation / cardiac muscle cell proliferation / regulation of T cell differentiation / regulation of axon extension / HDR through Single Strand Annealing (SSA) / positive regulation of cell migration involved in sprouting angiogenesis / negative regulation of cell-cell adhesion / Fc-gamma receptor signaling pathway involved in phagocytosis / BMP signaling pathway / Myogenesis / positive regulation of osteoblast proliferation / regulation of microtubule polymerization / RUNX2 regulates osteoblast differentiation / platelet-derived growth factor receptor-beta signaling pathway / peptidyl-tyrosine autophosphorylation / negative regulation of cellular senescence / positive regulation of focal adhesion assembly / associative learning / Bergmann glial cell differentiation / positive regulation of vasoconstriction / regulation of endocytosis / neuromuscular process controlling balance / actin monomer binding / negative regulation of long-term synaptic potentiation / endothelial cell migration / RHO GTPases Activate WASPs and WAVEs / positive regulation of T cell migration / signal transduction in response to DNA damage / negative regulation of double-strand break repair via homologous recombination / regulation of cell adhesion / mismatch repair / negative regulation of endothelial cell apoptotic process / canonical NF-kappaB signal transduction / four-way junction DNA binding / positive regulation of substrate adhesion-dependent cell spreading / spleen development / positive regulation of stress fiber assembly / cellular response to transforming growth factor beta stimulus / ruffle / positive regulation of establishment of T cell polarity / ERK1 and ERK2 cascade / positive regulation of interleukin-2 production / ephrin receptor binding / actin filament polymerization / phosphotyrosine residue binding / positive regulation of endothelial cell migration / response to endoplasmic reticulum stress / positive regulation of mitotic cell cycle / substrate adhesion-dependent cell spreading / SH2 domain binding / positive regulation of release of sequestered calcium ion into cytosol / post-embryonic development / thymus development / regulation of autophagy / neural tube closure / epidermal growth factor receptor signaling pathway / establishment of localization in cell / integrin-mediated signaling pathway / regulation of actin cytoskeleton organization 類似検索 - 分子機能 | ||||||
生物種 | Homo sapiens (ヒト) | ||||||
手法 | X線回折 / シンクロトロン / 分子置換 / 解像度: 1.65 Å | ||||||
データ登録者 | Pisabarro, M.T. / Serrano, L. / Wilmanns, M. | ||||||
引用 | ジャーナル: J.Mol.Biol. / 年: 1998 タイトル: Crystal structure of the abl-SH3 domain complexed with a designed high-affinity peptide ligand: implications for SH3-ligand interactions. 著者: Pisabarro, M.T. / Serrano, L. / Wilmanns, M. #1: ジャーナル: Biochemistry / 年: 1996 タイトル: Rational Design of Specific High-Affinity Peptide Ligands for the Abl-SH3 Domain 著者: Pisabarro, M.T. / Serrano, L. #2: ジャーナル: Nat.Struct.Biol. / 年: 1994 タイトル: High-Resolution Crystal Structures of Tyrosine Kinase SH3 Domains Complexed with Proline-Rich Peptides 著者: Musacchio, A. / Saraste, M. / Wilmanns, M. | ||||||
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 | 1bbz.cif.gz | 69.3 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb1bbz.ent.gz | 54.6 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 1bbz.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 | 1bbz_validation.pdf.gz | 442 KB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 1bbz_full_validation.pdf.gz | 451.9 KB | 表示 | |
XML形式データ | 1bbz_validation.xml.gz | 9.6 KB | 表示 | |
CIF形式データ | 1bbz_validation.cif.gz | 14.7 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/bb/1bbz ftp://data.pdbj.org/pub/pdb/validation_reports/bb/1bbz | HTTPS FTP |
-関連構造データ
関連構造データ | 1aboS S: 精密化の開始モデル |
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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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単位格子 |
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非結晶学的対称性 (NCS) | NCS oper:
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-要素
#1: タンパク質 | 分子量: 6423.080 Da / 分子数: 4 / 断片: SH3 DOMAIN / 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: P00519 #2: タンパク質・ペプチド | 分子量: 1035.149 Da / 分子数: 4 / 由来タイプ: 組換発現 #3: 化合物 | ChemComp-SO4 / #4: 水 | ChemComp-HOH / | |
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-実験情報
-実験
実験 | 手法: X線回折 / 使用した結晶の数: 1 |
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-試料調製
結晶 | マシュー密度: 2.31 Å3/Da / 溶媒含有率: 46.68 % | ||||||||||||||||||||||||||||||||||||
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結晶化 | 手法: 蒸気拡散法 / pH: 3.1 詳細: CRYSTALS WITH DIMENSIONS 0.25X0.25X0.25 MM3 WERE OBTAINED AT ROOM TEMPERATURE BY VAPOUR DIFFUSION AGAINST A RESERVOIR CONTAINING 0.1 M CITRIC ACID PH 3.1, 2 M AMMONIUM SULPHATE, 0.2 M SODIUM ...詳細: CRYSTALS WITH DIMENSIONS 0.25X0.25X0.25 MM3 WERE OBTAINED AT ROOM TEMPERATURE BY VAPOUR DIFFUSION AGAINST A RESERVOIR CONTAINING 0.1 M CITRIC ACID PH 3.1, 2 M AMMONIUM SULPHATE, 0.2 M SODIUM CHLORIDE, AND 1MM DTT/EDTA. THE HANGING DROP CONTAINED 1:1 RATIO OF RESERVOIR AND PROTEIN-PEPTIDE SOLUTIONS., vapor diffusion | ||||||||||||||||||||||||||||||||||||
結晶化 | *PLUS 手法: 蒸気拡散法, ハンギングドロップ法 | ||||||||||||||||||||||||||||||||||||
溶液の組成 | *PLUS
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-データ収集
回折 | 平均測定温度: 120 K |
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放射光源 | 由来: シンクロトロン / サイト: EMBL/DESY, HAMBURG / ビームライン: BW7B / 波長: 0.88 |
検出器 | タイプ: MARRESEARCH / 検出器: IMAGE PLATE / 日付: 1996年10月1日 |
放射 | 単色(M)・ラウエ(L): M / 散乱光タイプ: x-ray |
放射波長 | 波長: 0.88 Å / 相対比: 1 |
反射 | 解像度: 1.6→39.3 Å / Num. obs: 226846 / % possible obs: 99.7 % / Observed criterion σ(I): 0 / 冗長度: 6.59 % / Biso Wilson estimate: 15.4 Å2 / Rmerge(I) obs: 0.058 / Rsym value: 0.058 / Net I/σ(I): 15.1 |
反射 シェル | 解像度: 1.6→1.63 Å / 冗長度: 3.7 % / Rmerge(I) obs: 0.58 / Mean I/σ(I) obs: 1.9 / Rsym value: 0.58 / % possible all: 98.4 |
反射 | *PLUS Num. obs: 34430 / Num. measured all: 226846 |
-解析
ソフトウェア |
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精密化 | 構造決定の手法: 分子置換 開始モデル: 1ABO 解像度: 1.65→8 Å / 交差検証法: FREE R-FACTOR / σ(F): 1
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原子変位パラメータ | Biso mean: 13.5 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
精密化ステップ | サイクル: LAST / 解像度: 1.65→8 Å
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拘束条件 |
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Xplor file |
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