登録情報 | データベース: PDB / ID: 3bys |
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タイトル | co-crystal structure of Lck and aminopyrimidine amide 10b |
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要素 | Proto-oncogene tyrosine-protein kinase LCK |
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キーワード | TRANSFERASE / Lck / Kinase domain / Alternative splicing / ATP-binding / Chromosomal rearrangement / Cytoplasm / Disease mutation / Host-virus interaction / Lipoprotein / Membrane / Myristate / Nucleotide-binding / Palmitate / Phosphoprotein / Proto-oncogene / SH2 domain / SH3 domain / Tyrosine-protein kinase |
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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 / peptidyl-tyrosine autophosphorylation / 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 / 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 / peptidyl-tyrosine phosphorylation / Signaling by SCF-KIT / platelet activation / activation of cysteine-type endopeptidase activity involved in apoptotic process / Constitutive Signaling by Aberrant PI3K in Cancer / PIP3 activates AKT signaling / positive regulation of T cell activation / Downstream TCR signaling / DAP12 signaling / ATPase binding / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / T cell receptor signaling pathway / 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 / : / SH3 domain / SH2 domain / Src homology 2 (SH2) domain profile. / Src homology 2 domains / SH2 domain / Src homology 3 domains / SH2 domain superfamily ...Lck, SH3 domain / Tyrosine-protein kinase Lck, SH2 domain / : / 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 / Serine-threonine/tyrosine-protein kinase, catalytic domain / Protein tyrosine and serine/threonine kinase / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / 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 / Orthogonal Bundle / Mainly Alpha / 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 / 分子置換 / 解像度: 2.2 Å |
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データ登録者 | Huang, X. |
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引用 | ジャーナル: J.Med.Chem. / 年: 2008 タイトル: Structure-guided design of aminopyrimidine amides as potent, selective inhibitors of lymphocyte specific kinase: synthesis, structure-activity relationships, and inhibition of in vivo T cell activation. 著者: DiMauro, E.F. / Newcomb, J. / Nunes, J.J. / Bemis, J.E. / Boucher, C. / Chai, L. / Chaffee, S.C. / Deak, H.L. / Epstein, L.F. / Faust, T. / Gallant, P. / Gore, A. / Gu, Y. / Henkle, B. / ...著者: DiMauro, E.F. / Newcomb, J. / Nunes, J.J. / Bemis, J.E. / Boucher, C. / Chai, L. / Chaffee, S.C. / Deak, H.L. / Epstein, L.F. / Faust, T. / Gallant, P. / Gore, A. / Gu, Y. / Henkle, B. / Hsieh, F. / Huang, X. / Kim, J.L. / Lee, J.H. / Martin, M.W. / McGowan, D.C. / Metz, D. / Mohn, D. / Morgenstern, K.A. / Oliveira-dos-Santos, A. / Patel, V.F. / Powers, D. / Rose, P.E. / Schneider, S. / Tomlinson, S.A. / Tudor, Y.Y. / Turci, S.M. / Welcher, A.A. / Zhao, H. / Zhu, L. / Zhu, X. |
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履歴 | 登録 | 2008年1月16日 | 登録サイト: RCSB / 処理サイト: RCSB |
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改定 1.0 | 2008年9月16日 | Provider: repository / タイプ: Initial release |
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改定 1.1 | 2011年7月13日 | Group: Version format compliance |
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改定 1.2 | 2023年8月30日 | Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description カテゴリ: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id |
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