Diversity does make a difference: fibroblast growth factor-heparin interactions.
Fibroblast growth factors (FGFs) are members of a protein family with a broad range of biological activities. The best characterized FGFs interact with two distinct extracellular receptors--a transmembrane tyrosine kinase FGF receptor (FGFR) and a heparan f1p4ate-related proteoglycan of the extracellular matrix. These components form a FGF-FGFR-proteoglycan complex that activates the FGF-mediated signal transduction process through FGFR dimerization. Recent crystal structure determinations of FGF-heparin complexes have provided insights into both the interactions between these components and the role of heparin-like proteoglycans in FGF function. Future advances in this field will benefit enormously from an ability to specifically prepare homogeneous heparin-based oligosaccharides of defined sequence for use in biochemical and structural studies of FGF and many other systems.
Faham
S
S
Department of Chemistry and Biochemistry, University of California, Los Angeles 90095-1570, USA. salem@ewald.mbi.ucla.edu
Linhardt
R J
RJ
Rees
D C
DC
D001665:Binding Sites; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D005346:Fibroblast Growth Factors / Q000737:chemistry* / Q000378:metabolism*; D006493:Heparin / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D015398:Signal Transduction
D005346:Fibroblast Growth Factors; D006493:Heparin