Entry Database : PDB / ID : 4xsk Structure visualization Downloads & linksTitle Structure of PAItrap, an uPA mutant ComponentsUrokinase-type plasminogen activator Details Keywords BLOOD CLOTTING / antagonist / PAI-1 / uPAFunction / homology Function and homology informationFunction Domain/homology Component
u-plasminogen activator / regulation of smooth muscle cell-matrix adhesion / urokinase plasminogen activator signaling pathway / regulation of plasminogen activation / regulation of fibrinolysis / regulation of wound healing / protein complex involved in cell-matrix adhesion / negative regulation of plasminogen activation / regulation of smooth muscle cell migration / regulation of signaling receptor activity ... u-plasminogen activator / regulation of smooth muscle cell-matrix adhesion / urokinase plasminogen activator signaling pathway / regulation of plasminogen activation / regulation of fibrinolysis / regulation of wound healing / protein complex involved in cell-matrix adhesion / negative regulation of plasminogen activation / regulation of smooth muscle cell migration / regulation of signaling receptor activity / serine-type endopeptidase complex / Dissolution of Fibrin Clot / smooth muscle cell migration / plasminogen activation / regulation of cell adhesion mediated by integrin / tertiary granule membrane / negative regulation of fibrinolysis / regulation of cell adhesion / specific granule membrane / serine protease inhibitor complex / fibrinolysis / chemotaxis / blood coagulation / regulation of cell population proliferation / response to hypoxia / positive regulation of cell migration / external side of plasma membrane / serine-type endopeptidase activity / focal adhesion / Neutrophil degranulation / cell surface / signal transduction / proteolysis / extracellular space / extracellular exosome / extracellular region / plasma membrane Similarity search - Function Kringle domain / Kringle / Kringle, conserved site / Kringle superfamily / Kringle domain signature. / Kringle domain profile. / Kringle domain / : / Kringle-like fold / EGF-like domain profile. ... Kringle domain / Kringle / Kringle, conserved site / Kringle superfamily / Kringle domain signature. / Kringle domain profile. / Kringle domain / : / Kringle-like fold / EGF-like domain profile. / EGF-like domain signature 1. / EGF-like domain / Serine proteases, trypsin family, histidine active site / Serine proteases, trypsin family, serine active site / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin family, histidine active site. / Serine proteases, trypsin domain profile. / Serine proteases, trypsin family, serine active site. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / Trypsin-like serine proteases / Thrombin, subunit H / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / Beta Barrel / Mainly Beta Similarity search - Domain/homologyBiological species Homo sapiens (human)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 1.5 Å DetailsAuthors Gong, L. / Proulle, V. / Hong, Z. / Lin, Z. / Liu, M. / Yuan, C. / Lin, L. / Furie, B. / Flaumenhaft, R. / Andreasen, P. ...Gong, L. / Proulle, V. / Hong, Z. / Lin, Z. / Liu, M. / Yuan, C. / Lin, L. / Furie, B. / Flaumenhaft, R. / Andreasen, P. / Furie, B. / Huang, M. Funding support China, United States, 6items Details Hide detailsOrganization Grant number Country National Natural Science Foundation of China 31161130356 China NFSC 31370737 China National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI) HL087203 United States National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI) HL095084 United States CAS/SFEA International Partnership Program for Creative Research Teams China NSF of Fujian Province 2012J05071 China
CitationJournal : To Be Published Title : Structure of PAItrap, an uPA mutantAuthors : Gong, L. / Proulle, V. / Hong, Z. / Lin, Z. / Liu, M. / Yuan, C. / Lin, L. / Furie, B. / Flaumenhaft, R. / Andreasen, P. / Furie, B. / Huang, M. History Deposition Jan 22, 2015 Deposition site : RCSB / Processing site : PDBJRevision 1.0 Feb 3, 2016 Provider : repository / Type : Initial releaseRevision 1.1 Oct 18, 2017 Group : Author supporting evidence / Derived calculations / Category : pdbx_audit_support / pdbx_struct_oper_listItem : _pdbx_audit_support.funding_organization / _pdbx_struct_oper_list.symmetry_operationRevision 1.2 Mar 23, 2022 Group : Author supporting evidence / Database references / Category : database_2 / pdbx_audit_supportItem : _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_audit_support.funding_organizationRevision 1.3 Nov 8, 2023 Group : Data collection / Refinement descriptionCategory : chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model
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