RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/18174166http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18174166http://www.w3.org/2000/01/rdf-schema#comment"Vitronectin and plasminogen activator inhibitor-1 (PAI-1) are important physiological binding partners that work in concert to regulate cellular adhesion, migration, and fibrinolysis. The high affinity binding site for PAI-1 is located within the N-terminal somatomedin B domain of vitronectin; however, several studies have suggested a second PAI-1-binding site within vitronectin. To investigate this secondary site, a vitronectin mutant lacking the somatomedin B domain (rDeltasBVN) was engineered. The short deletion had no effect on heparin-binding, integrin-binding, or cellular adhesion. Binding to the urokinase receptor was completely abolished while PAI-1 binding was still observed, albeit with a lower affinity. Analytical ultracentrifugation on the PAI-1-vitronectin complex demonstrated that increasing NaCl concentration favors 1:1 versus 2:1 PAI-1-vitronectin complexes and hampers formation of higher order complexes, pointing to the contribution of charge-charge interactions for PAI-1 binding to the second site. Furthermore, fluorescence resonance energy transfer between differentially labeled PAI-1 molecules confirmed that two independent molecules of PAI-1 are capable of binding to vitronectin. These results support a model for the assembly of higher order PAI-1-vitronectin complexes via two distinct binding sites in both proteins."xsd:string
http://purl.uniprot.org/citations/18174166http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m708017200"xsd:string
http://purl.uniprot.org/citations/18174166http://purl.uniprot.org/core/author"Peterson C.B."xsd:string
http://purl.uniprot.org/citations/18174166http://purl.uniprot.org/core/author"Minor K.H."xsd:string
http://purl.uniprot.org/citations/18174166http://purl.uniprot.org/core/author"Blouse G.E."xsd:string
http://purl.uniprot.org/citations/18174166http://purl.uniprot.org/core/author"Schar C.R."xsd:string
http://purl.uniprot.org/citations/18174166http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18174166http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/18174166http://purl.uniprot.org/core/pages"10297-10309"xsd:string
http://purl.uniprot.org/citations/18174166http://purl.uniprot.org/core/title"A deletion mutant of vitronectin lacking the somatomedin B domain exhibits residual plasminogen activator inhibitor-1-binding activity."xsd:string
http://purl.uniprot.org/citations/18174166http://purl.uniprot.org/core/volume"283"xsd:string
http://purl.uniprot.org/citations/18174166http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18174166
http://purl.uniprot.org/citations/18174166http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18174166
http://purl.uniprot.org/uniprot/#_B7Z553-mappedCitation-18174166http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18174166
http://purl.uniprot.org/uniprot/#_D9ZGG2-mappedCitation-18174166http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18174166
http://purl.uniprot.org/uniprot/#_J7HH10-mappedCitation-18174166http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18174166
http://purl.uniprot.org/uniprot/#_P04004-mappedCitation-18174166http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18174166
http://purl.uniprot.org/uniprot/J7HH10http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18174166
http://purl.uniprot.org/uniprot/B7Z553http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18174166
http://purl.uniprot.org/uniprot/D9ZGG2http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18174166
http://purl.uniprot.org/uniprot/P04004http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18174166