登録情報 | データベース: PDB / ID: 1fbz |
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タイトル | Structure-based design of a novel, osteoclast-selective, nonpeptide Src SH2 inhibitor with in vivo anti-resorptive activity |
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要素 | PROTO-ONCOGENE TYROSINE-PROTEIN KINASE LCK |
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キーワード | TRANSFERASE / SH2 DOMAIN / NONPEPTIDE INHIBITOR |
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機能・相同性 | 機能・相同性情報
regulation of lymphocyte activation / positive regulation of leukocyte cell-cell adhesion / Fc-gamma receptor signaling pathway / CD28 co-stimulation / FLT3 signaling through SRC family kinases / intracellular zinc ion homeostasis / CD4 receptor binding / Nef Mediated CD4 Down-regulation / Nef and signal transduction / positive regulation of heterotypic cell-cell adhesion ...regulation of lymphocyte activation / positive regulation of leukocyte cell-cell adhesion / Fc-gamma receptor signaling pathway / CD28 co-stimulation / FLT3 signaling through SRC family kinases / intracellular zinc ion homeostasis / CD4 receptor binding / Nef Mediated CD4 Down-regulation / Nef and signal transduction / positive regulation of heterotypic cell-cell adhesion / Interleukin-2 signaling / CD28 dependent Vav1 pathway / Regulation of KIT signaling / CTLA4 inhibitory signaling / protein serine/threonine phosphatase activity / phospholipase activator activity / leukocyte migration / CD8 receptor binding / pericentriolar material / positive regulation of T cell receptor signaling pathway / Translocation of ZAP-70 to Immunological synapse / Phosphorylation of CD3 and TCR zeta chains / PECAM1 interactions / CD28 dependent PI3K/Akt signaling / phospholipase binding / hemopoiesis / RHOH GTPase cycle / Generation of second messenger molecules / immunological synapse / T cell differentiation / PD-1 signaling / phosphatidylinositol 3-kinase binding / T cell receptor binding / peptidyl-tyrosine autophosphorylation / positive regulation of intrinsic apoptotic signaling pathway / release of sequestered calcium ion into cytosol / cell surface receptor protein tyrosine kinase signaling pathway / GPVI-mediated activation cascade / T cell costimulation / phosphotyrosine residue binding / SH2 domain binding / Signaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT mutants / B cell receptor signaling pathway / non-specific protein-tyrosine kinase / non-membrane spanning protein tyrosine kinase activity / Signaling by SCF-KIT / platelet activation / peptidyl-tyrosine phosphorylation / Constitutive Signaling by Aberrant PI3K in Cancer / activation of cysteine-type endopeptidase activity involved in apoptotic process / positive regulation of T cell activation / Downstream TCR signaling / DAP12 signaling / PIP3 activates AKT signaling / T cell receptor signaling pathway / ATPase binding / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / protein phosphatase binding / protein tyrosine kinase activity / intracellular signal transduction / response to xenobiotic stimulus / membrane raft / protein phosphorylation / innate immune response / signaling receptor binding / protein kinase binding / extracellular exosome / ATP binding / identical protein binding / plasma membrane / cytosol類似検索 - 分子機能 Lck, SH3 domain / Tyrosine-protein kinase Lck, SH2 domain / SH2 domain / SHC Adaptor Protein / : / SH3 domain / SH2 domain / Src homology 2 (SH2) domain profile. / Src homology 2 domains / SH2 domain ...Lck, SH3 domain / Tyrosine-protein kinase Lck, SH2 domain / SH2 domain / SHC Adaptor Protein / : / SH3 domain / SH2 domain / Src homology 2 (SH2) domain profile. / Src homology 2 domains / SH2 domain / Src homology 3 domains / SH2 domain superfamily / SH3-like domain superfamily / Src homology 3 (SH3) domain profile. / SH3 domain / Tyrosine-protein kinase, catalytic domain / Tyrosine kinase, catalytic domain / Tyrosine protein kinases specific active-site signature. / Tyrosine-protein kinase, active site / Protein tyrosine and serine/threonine kinase / Serine-threonine/tyrosine-protein kinase, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / 2-Layer Sandwich / Alpha Beta類似検索 - ドメイン・相同性 |
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生物種 | Homo sapiens (ヒト) |
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手法 | X線回折 / 解像度: 2.4 Å |
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データ登録者 | Shakespeare, W. / Yang, M. / Bohacek, R. / Cerasoli, F. / Stebbis, K. / Sundaramoorthi, R. / Vu, C. / Pradeepan, S. / Metcalf, C. / Haraldson, C. ...Shakespeare, W. / Yang, M. / Bohacek, R. / Cerasoli, F. / Stebbis, K. / Sundaramoorthi, R. / Vu, C. / Pradeepan, S. / Metcalf, C. / Haraldson, C. / Merry, T. / Dalgarno, D. / Narula, S. / Hatada, M. / Lu, X. / Van Schravendijk, M.R. / Adams, S. / Violette, S. / Smith, J. / Guan, W. / Bartlett, C. / Herson, J. / Iuliucci, J. / Weigele, M. / Sawyer, T. |
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引用 | ジャーナル: Proc.Natl.Acad.Sci.Usa / 年: 2000 タイトル: Structure-based design of an osteoclast-selective, nonpeptide src homology 2 inhibitor with in vivo antiresorptive activity. 著者: Shakespeare, W. / Yang, M. / Bohacek, R. / Cerasoli, F. / Stebbins, K. / Sundaramoorthi, R. / Azimioara, M. / Vu, C. / Pradeepan, S. / Metcalf, C. / Haraldson, C. / Merry, T. / Dalgarno, D. / ...著者: Shakespeare, W. / Yang, M. / Bohacek, R. / Cerasoli, F. / Stebbins, K. / Sundaramoorthi, R. / Azimioara, M. / Vu, C. / Pradeepan, S. / Metcalf, C. / Haraldson, C. / Merry, T. / Dalgarno, D. / Narula, S. / Hatada, M. / Lu, X. / van Schravendijk, M.R. / Adams, S. / Violette, S. / Smith, J. / Guan, W. / Bartlett, C. / Herson, J. / Iuliucci, J. / Weigele, M. / Sawyer, T. |
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履歴 | 登録 | 2000年7月17日 | 登録サイト: RCSB / 処理サイト: RCSB |
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改定 1.0 | 2000年8月23日 | Provider: repository / タイプ: Initial release |
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改定 1.1 | 2008年4月27日 | Group: Version format compliance |
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改定 1.2 | 2011年7月13日 | Group: Version format compliance |
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改定 1.3 | 2024年2月7日 | Group: Data collection / Database references / Derived calculations カテゴリ: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_ref_seq_dif / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id |
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