Heparin structure and interactions with basic fibroblast growth factor

S. Faham, R. E. Hileman, J. R. Fromm, R. J. Linhardt, D. C. Rees

Research output: Contribution to journalArticlepeer-review

752 Scopus citations

Abstract

Crystal structures of heparin-derived tetra- and hexasaccharides complexed with basic fibroblast growth factor (bFGF) were determined at resolutions of 1.9 and 2.2 angstroms, respectively. The heparin structure may be approximated as a helical polymer with a disaccharide rotation of 174° and a translation of 8.6 angstroms along the helix axis. Both molecules bound similarly to a region of the bFGF surface containing residues asparagine-28, arginine-121, lysine-126 and glutamine-135; the hexasaccharide also interacted with an additional binding site formed by lysine-27, asparagine-102, and lysine-136. No significant conformational change in bFGF occurred upon heparin oligosaccharide binding, which suggests that heparin primarily serves to juxtapose components of the FGF signal transduction pathway.

Original languageEnglish
Pages (from-to)1116-1120
Number of pages5
JournalScience
Volume271
Issue number5252
DOIs
StatePublished - 23 Feb 1996
Externally publishedYes

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