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http://purl.uniprot.org/citations/16257968http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16257968http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16257968http://www.w3.org/2000/01/rdf-schema#comment"Fibroblast growth factor-binding proteins (FGF-BP) are secreted carrier proteins that release fibroblast growth factors (FGFs) from the extracellular matrix storage and thus enhance FGF activity. Here we have mapped the interaction domain between human FGF-BP1 and FGF-2. For this, we generated T7 phage display libraries of N-terminally and C-terminally truncated FGF-BP1 fragments that were then panned against immobilized FGF-2. From this panning, a C-terminal fragment of FGF-BP1 (amino acids 193-234) was identified as the minimum binding domain for FGF. As a recombinant protein, this C-terminal fragment binds to FGF-2 and enhances FGF-2-induced signaling in NIH-3T3 fibroblasts and GM7373 endothelial cells, as well as mitogenesis and chemotaxis of NIH-3T3 cells. The FGF interaction domain in FGF-BP1 is distinct from the heparin-binding domain (amino acids 110-143), and homology modeling supports the notion of a distinct domain in the C terminus that is conserved across different species. This domain also contains conserved positioning of cysteine residues with the Cys-214/Cys-222 positions in the human protein predicted to participate in disulfide bridge formation. Phage display of a C214A mutation of FGF-BP1 reduced binding to FGF-2, indicating the functional significance of this disulfide bond. We concluded that the FGF interaction domain is contained in the C terminus of FGF-BP1."xsd:string
http://purl.uniprot.org/citations/16257968http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m510754200"xsd:string
http://purl.uniprot.org/citations/16257968http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m510754200"xsd:string
http://purl.uniprot.org/citations/16257968http://purl.uniprot.org/core/author"Wang S."xsd:string
http://purl.uniprot.org/citations/16257968http://purl.uniprot.org/core/author"Wang S."xsd:string
http://purl.uniprot.org/citations/16257968http://purl.uniprot.org/core/author"Ueda Y."xsd:string
http://purl.uniprot.org/citations/16257968http://purl.uniprot.org/core/author"Ueda Y."xsd:string
http://purl.uniprot.org/citations/16257968http://purl.uniprot.org/core/author"Xie B."xsd:string
http://purl.uniprot.org/citations/16257968http://purl.uniprot.org/core/author"Xie B."xsd:string
http://purl.uniprot.org/citations/16257968http://purl.uniprot.org/core/author"Tomita Y."xsd:string
http://purl.uniprot.org/citations/16257968http://purl.uniprot.org/core/author"Tomita Y."xsd:string
http://purl.uniprot.org/citations/16257968http://purl.uniprot.org/core/author"Tassi E."xsd:string
http://purl.uniprot.org/citations/16257968http://purl.uniprot.org/core/author"Tassi E."xsd:string
http://purl.uniprot.org/citations/16257968http://purl.uniprot.org/core/author"McDonnell K."xsd:string
http://purl.uniprot.org/citations/16257968http://purl.uniprot.org/core/author"McDonnell K."xsd:string
http://purl.uniprot.org/citations/16257968http://purl.uniprot.org/core/author"Bowden E.T."xsd:string
http://purl.uniprot.org/citations/16257968http://purl.uniprot.org/core/author"Bowden E.T."xsd:string
http://purl.uniprot.org/citations/16257968http://purl.uniprot.org/core/author"Riegel A.T."xsd:string
http://purl.uniprot.org/citations/16257968http://purl.uniprot.org/core/author"Riegel A.T."xsd:string
http://purl.uniprot.org/citations/16257968http://purl.uniprot.org/core/author"Wellstein A."xsd:string
http://purl.uniprot.org/citations/16257968http://purl.uniprot.org/core/author"Wellstein A."xsd:string
http://purl.uniprot.org/citations/16257968http://purl.uniprot.org/core/author"Swift M.R."xsd:string
http://purl.uniprot.org/citations/16257968http://purl.uniprot.org/core/author"Swift M.R."xsd:string