1bfb: Difference between revisions
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|PDB= 1bfb |SIZE=350|CAPTION= <scene name='initialview01'>1bfb</scene>, resolution 1.9Å | |PDB= 1bfb |SIZE=350|CAPTION= <scene name='initialview01'>1bfb</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=IDU:1,4-DIDEOXY-O2-SULFO-GLUCURONIC+ACID'>IDU</scene>, <scene name='pdbligand=SGN:N,O6-DISULFO-GLUCOSAMINE'>SGN</scene>, <scene name='pdbligand=UAP:1,4-DIDEOXY-5-DEHYDRO-O2-SULFO-GLUCURONIC+ACID'>UAP</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bfb OCA], [http://www.ebi.ac.uk/pdbsum/1bfb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bfb RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==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. | 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== | ==About this Structure== | ||
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[[Category: Rees, D C.]] | [[Category: Rees, D C.]] | ||
[[Category: growth factor]] | [[Category: growth factor]] | ||
[[Category: heparin-binding]] | [[Category: heparin-binding,]] | ||
[[Category: mitogen]] | [[Category: mitogen]] | ||
[[Category: vascularization]] | [[Category: vascularization]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:59:44 2008'' | ||
