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Interactions of putative heparin-binding domains of basic fibroblast growth factor and its receptor, FGFR-1, with
L Kinsella1, H L Chen, J A Smith
1Cancer Laboratory, School of Biological Sciences, Liverpool, UK.
Glycoconjugate Journal
|June 5, 1998
Abstract:
We have examined structure-function relationships that have been proposed to account for the heparin-binding properties of basic fibroblast growth factor and its receptor, FGFR-1, using synthetic peptides, DNA synthesis assays and binding assays in a resonant mirror biosensor. The results suggest that the interaction of FGFR-1 with heparin may not be physiologically relevant and that the site of interaction of the polysaccharide on bFGF is more complex than has been anticipated.