1bfc
From Proteopedia
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| , resolution 2.2Å | |||||||
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| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BASIC FIBROBLAST GROWTH FACTOR COMPLEXED WITH HEPARIN HEXAMER FRAGMENT
Overview
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.
About this Structure
1BFC is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Mar 30 18:59:44 2008
