登録情報 | データベース: PDB / ID: 1x27 |
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タイトル | Crystal Structure of Lck SH2-SH3 with SH2 binding site of p130Cas |
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要素 | - CRK-associated substrate
- Proto-oncogene tyrosine-protein kinase LCK
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キーワード | SIGNALING PROTEIN / Lck-Cas complex / LCK phospho-peptide complex / High affinity LCK-Cas complex |
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機能・相同性 | 機能・相同性情報
p130Cas linkage to MAPK signaling for integrins / PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases / VEGFA-VEGFR2 Pathway / Downstream signal transduction / antigen receptor-mediated signaling pathway / cellular response to endothelin / regulation of lymphocyte activation / positive regulation of leukocyte cell-cell adhesion / negative regulation of substrate adhesion-dependent cell spreading / endothelin receptor signaling pathway ...p130Cas linkage to MAPK signaling for integrins / PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases / VEGFA-VEGFR2 Pathway / Downstream signal transduction / antigen receptor-mediated signaling pathway / cellular response to endothelin / regulation of lymphocyte activation / positive regulation of leukocyte cell-cell adhesion / negative regulation of substrate adhesion-dependent cell spreading / endothelin receptor signaling pathway / Fc-gamma receptor signaling pathway / hepatocyte growth factor receptor signaling pathway / CD28 co-stimulation / intracellular zinc ion homeostasis / FLT3 signaling through SRC family kinases / 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 / cellular response to hepatocyte growth factor stimulus / CTLA4 inhibitory signaling / protein serine/threonine phosphatase activity / leukocyte migration / phospholipase activator activity / 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 / neurotrophin TRK receptor signaling pathway / RHOH GTPase cycle / platelet-derived growth factor receptor signaling pathway / hemopoiesis / Generation of second messenger molecules / immunological synapse / T cell differentiation / PD-1 signaling / cellular response to nitric oxide / vascular endothelial growth factor receptor signaling pathway / phosphatidylinositol 3-kinase binding / T cell receptor binding / positive regulation of intrinsic apoptotic signaling pathway / peptidyl-tyrosine autophosphorylation / release of sequestered calcium ion into cytosol / extrinsic component of cytoplasmic side of plasma membrane / GPVI-mediated activation cascade / ruffle / cell surface receptor protein tyrosine kinase signaling pathway / T cell costimulation / phosphotyrosine residue binding / positive regulation of endothelial cell migration / SH2 domain binding / cell chemotaxis / Signaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT mutants / integrin-mediated signaling pathway / actin filament organization / B cell receptor signaling pathway / non-specific protein-tyrosine kinase / non-membrane spanning protein tyrosine kinase activity / epidermal growth factor receptor signaling pathway / Signaling by SCF-KIT / platelet activation / SH3 domain binding / peptidyl-tyrosine phosphorylation / Constitutive Signaling by Aberrant PI3K in Cancer / activation of cysteine-type endopeptidase activity involved in apoptotic process / cell migration / actin cytoskeleton / Downstream TCR signaling / positive regulation of T cell activation / insulin receptor signaling pathway / PIP3 activates AKT signaling / DAP12 signaling / lamellipodium / T cell receptor signaling pathway / ATPase binding / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / actin cytoskeleton organization / protein phosphatase binding / protein tyrosine kinase activity / cell adhesion / intracellular signal transduction / positive regulation of cell migration / response to xenobiotic stimulus / membrane raft / G protein-coupled receptor signaling pathway / protein domain specific binding / axon / protein phosphorylation / innate immune response / focal adhesion / signaling receptor binding / protein kinase binding / extracellular exosome類似検索 - 分子機能 : / BCAR1, SH3 domain / Serine rich protein interaction domain / CAS family, C-terminal / CAS family / CAS, serine rich four helix bundle domain superfamily / Serine rich protein interaction domain / Crk-Associated Substrate C-terminal domain / Lck, SH3 domain / Tyrosine-protein kinase Lck, SH2 domain ...: / BCAR1, SH3 domain / Serine rich protein interaction domain / CAS family, C-terminal / CAS family / CAS, serine rich four helix bundle domain superfamily / Serine rich protein interaction domain / Crk-Associated Substrate C-terminal domain / Lck, SH3 domain / Tyrosine-protein kinase Lck, SH2 domain / SH2 domain / SHC Adaptor Protein / SH3 Domains / SH3 domain / SH2 domain / Src homology 2 (SH2) domain profile. / Src homology 2 domains / SH3 type barrels. / 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 / Roll / 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 / Mainly Beta / Alpha Beta類似検索 - ドメイン・相同性 Tyrosine-protein kinase Lck / Breast cancer anti-estrogen resistance protein 1類似検索 - 構成要素 |
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生物種 | Homo sapiens (ヒト) |
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手法 | X線回折 / シンクロトロン / 分子置換 / 解像度: 2.7 Å |
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データ登録者 | Nasertorabi, F. / Tars, K. / Becherer, K. / Kodandapani, R. / Liljas, L. / Vuori, K. / Ely, K.R. |
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引用 | ジャーナル: J.MOL.RECOG. / 年: 2006 タイトル: Molecular basis for regulation of Src by the docking protein p130Cas 著者: Nasertorabi, F. / Tars, K. / Becherer, K. / Kodandapani, R. / Liljas, L. / Vuori, K. / Ely, K.R. |
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履歴 | 登録 | 2005年4月20日 | 登録サイト: PDBJ / 処理サイト: PDBJ |
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改定 1.0 | 2006年2月7日 | Provider: repository / タイプ: Initial release |
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改定 1.1 | 2008年4月30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 | 2023年10月25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 / pdbx_struct_conn_angle / struct_conn / struct_conn_type / 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 / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_conn_type.id / _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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改定 1.4 | 2023年11月15日 | Group: Data collection / カテゴリ: chem_comp_atom / chem_comp_bond / Item: _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_2 |
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