1BFC

BASIC FIBROBLAST GROWTH FACTOR COMPLEXED WITH HEPARIN HEXAMER FRAGMENT

Summary for 1BFC

• Entry DOI: 10.2210/pdb1bfc/pdb
• Descriptor: BASIC FIBROBLAST GROWTH FACTOR, 4-deoxy-2-O-sulfo-alpha-L-threo-hex-4-enopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose (3 entities in total)
• Functional Keywords: growth factor, mitogen, vascularization, heparin-binding
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 18249.29

Authors

Faham, S.,Rees, D.C. (deposition date: 1995-12-12, release date: 1996-04-03, Last modification date: 2024-02-07)

Primary citation

Faham, S.,Hileman, R.E.,Fromm, J.R.,Linhardt, R.J.,Rees, D.C.
Heparin structure and interactions with basic fibroblast growth factor.
Science, 271:1116-1120, 1996

PubMed 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 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.

PubMed: 8599088

Experimental method

X-RAY DIFFRACTION (2.2 Å)