Diversity does make a difference: fibroblast growth factor-heparin interactions.

S Faham; R J Linhardt; D C Rees

doi:10.1016/s0959-440x(98)80147-4

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Diversity does make a difference: fibroblast growth factor-heparin interactions.

S Faham·R J Linhardt·D C Rees

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Abstract

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.

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Binding Sites Carbohydrate Conformation Carbohydrate Sequence Fibroblast Growth Factors Heparin Models, Molecular Molecular Sequence Data Protein Conformation Signal Transduction Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.Review

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S Faham, R J Linhardt, D C Rees. 1998. Diversity does make a difference: fibroblast growth factor-heparin interactions.. https://doi.org/10.1016/s0959-440x(98)80147-4

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