2erm
Solution structure of a biologically active human FGF-1 monomer, complexed to a hexasaccharide heparin-analogue
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OverviewOverview
The 3D structure of a complex formed by the acidic fibroblast growth, factor (FGF-1) and a specifically designed synthetic heparin, hexasaccharide has been determined by NMR spectroscopy. This, hexasaccharide can substitute natural heparins in FGF-1 mitogenesis, assays, in spite of not inducing any apparent dimerization of the growth, factor. The use of this well defined synthetic heparin analogue has, allowed us to perform a detailed NMR structural analysis of the, heparin-FGF interaction, overcoming the limitations of NMR to deal with, the high molecular mass and heterogeneity of the FGF-1 oligomers formed in, the presence of natural heparin fragments. Our results confirm that, glycosaminoglycans induced FGF-1 dimerization either in a cis or trans, disposition with respect to the heparin chain is not an absolute, requirement for biological activity.
DiseaseDisease
Known diseases associated with this structure: Aplasia of lacrimal and salivary glands OMIM:[602115], LADD syndrome OMIM:[602115]
About this StructureAbout this Structure
2ERM is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Solution NMR structure of a human FGF-1 monomer, activated by a hexasaccharide heparin-analogue., Canales A, Lozano R, Lopez-Mendez B, Angulo J, Ojeda R, Nieto PM, Martin-Lomas M, Gimenez-Gallego G, Jimenez-Barbero J, FEBS J. 2006 Oct;273(20):4716-27. Epub 2006 Sep 21. PMID:16995857
Page seeded by OCA on Fri Feb 15 17:23:46 2008