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http://purl.uniprot.org/citations/1709159http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1709159http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1709159http://www.w3.org/2000/01/rdf-schema#comment"High affinity binding of platelet-derived growth factor (PDGF) has been proposed to involve the interaction of the dimeric PDGF ligand with two receptor subunits, designated alpha and beta. We have cloned and expressed a human PDGF receptor cDNA which differs in sequence from the beta-subunit and which has the PDGF binding properties and monoclonal antibody recognition, predicted for the alpha-subunit. Scatchard analysis indicated that PDGF-AA and PDGF-AB bound to transfected alpha-subunits with affinities of Kd = 0.06 and 0.05 nM, respectively. PDGF-BB bound with a significantly lower affinity (Kd = 0.4 nM). Nevertheless, this affinity is still great enough to mediate substantial PDGF-BB binding at physiological concentrations and would be considered to be "high affinity." We have used wild-type and kinase-inactive human beta-subunits to show that PDGF binding promotes receptor subunit dimerization in intact cells. In addition, we found that PDGF stimulates tyrosine phosphorylation of the kinase-inactive beta-subunit when it is expressed with alpha-subunits. The kinase-inactive beta-subunits were phosphorylated at tyrosine 857 and 751, the major phosphorylation sites of the wild-type beta-subunit, indicating either that intra- and intermolecular phosphorylation occurs on the same sites, or that a significant fraction of receptor tyrosine phosphorylation is intermolecular."xsd:string
http://purl.uniprot.org/citations/1709159http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(18)31541-2"xsd:string
http://purl.uniprot.org/citations/1709159http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(18)31541-2"xsd:string
http://purl.uniprot.org/citations/1709159http://purl.uniprot.org/core/author"Cooper J.A."xsd:string
http://purl.uniprot.org/citations/1709159http://purl.uniprot.org/core/author"Cooper J.A."xsd:string
http://purl.uniprot.org/citations/1709159http://purl.uniprot.org/core/author"Kazlauskas A."xsd:string
http://purl.uniprot.org/citations/1709159http://purl.uniprot.org/core/author"Kazlauskas A."xsd:string
http://purl.uniprot.org/citations/1709159http://purl.uniprot.org/core/author"Kelly J.D."xsd:string
http://purl.uniprot.org/citations/1709159http://purl.uniprot.org/core/author"Kelly J.D."xsd:string
http://purl.uniprot.org/citations/1709159http://purl.uniprot.org/core/author"Grant F.J."xsd:string
http://purl.uniprot.org/citations/1709159http://purl.uniprot.org/core/author"Grant F.J."xsd:string
http://purl.uniprot.org/citations/1709159http://purl.uniprot.org/core/author"Murray M.J."xsd:string
http://purl.uniprot.org/citations/1709159http://purl.uniprot.org/core/author"Murray M.J."xsd:string
http://purl.uniprot.org/citations/1709159http://purl.uniprot.org/core/author"Haldeman B.A."xsd:string
http://purl.uniprot.org/citations/1709159http://purl.uniprot.org/core/author"Haldeman B.A."xsd:string
http://purl.uniprot.org/citations/1709159http://purl.uniprot.org/core/author"Bowen-Pope D.F."xsd:string
http://purl.uniprot.org/citations/1709159http://purl.uniprot.org/core/author"Bowen-Pope D.F."xsd:string
http://purl.uniprot.org/citations/1709159http://purl.uniprot.org/core/author"Seifert R.A."xsd:string
http://purl.uniprot.org/citations/1709159http://purl.uniprot.org/core/author"Seifert R.A."xsd:string
http://purl.uniprot.org/citations/1709159http://purl.uniprot.org/core/date"1991"xsd:gYear
http://purl.uniprot.org/citations/1709159http://purl.uniprot.org/core/date"1991"xsd:gYear
http://purl.uniprot.org/citations/1709159http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/1709159http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string