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Solution structure of a biologically active human FGF-1 monomer, complexed to a hexasaccharide heparin-analogueSolution structure of a biologically active human FGF-1 monomer, complexed to a hexasaccharide heparin-analogue
Structural highlights
Function[FGF1_HUMAN] Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as potent mitogen in vitro.[1] [2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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