1bfb

Publication Abstract from PubMed

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 degrees 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.

Heparin structure and interactions with basic fibroblast growth factor.,Faham S, Hileman RE, Fromm JR, Linhardt RJ, Rees DC Science. 1996 Feb 23;271(5252):1116-20. PMID:8599088^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.