1bfc
From Proteopedia
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| - | [[Image:1bfc.gif|left|200px]] | + | [[Image:1bfc.gif|left|200px]] |
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| - | '''BASIC FIBROBLAST GROWTH FACTOR COMPLEXED WITH HEPARIN HEXAMER FRAGMENT''' | + | {{Structure |
| + | |PDB= 1bfc |SIZE=350|CAPTION= <scene name='initialview01'>1bfc</scene>, resolution 2.2Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''BASIC FIBROBLAST GROWTH FACTOR COMPLEXED WITH HEPARIN HEXAMER FRAGMENT''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BFC is a [ | + | 1BFC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BFC OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8599088 8599088] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: vascularization]] | [[Category: vascularization]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:10:14 2008'' |
Revision as of 08:10, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
BASIC FIBROBLAST GROWTH FACTOR COMPLEXED WITH HEPARIN HEXAMER FRAGMENT
Contents |
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.
Disease
Known diseases associated with this structure: Hypophosphatemic rickets, autosomal dominant OMIM:[605380], Osteomalacia, tumor-induced OMIM:[605380], Tumoral calcinosis, hyperphosphatemic, familial OMIM:[605380]
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 Thu Mar 20 10:10:14 2008
