tailieunhanh - Báo cáo khoa học: Solution NMR structure of a human FGF-1 monomer, activated by a hexasaccharide heparin-analogue

The 3D structure of a complex formed by the acidic fibroblast growth fac-tor (FGF-1) and a specifically designed synthetic heparin hexasaccharide has been determined by NMR spectroscopy. This hexasaccharide can sub-stitute natural heparins in FGF-1 mitogenesis assays, in spite of not indu-cing any apparent dimerization of the growth factor. | ễFEBS Journal Solution NMR structure of a human FGF-1 monomer activated by a hexasaccharide heparin-analogue Angeles Canales1 Rosa Lozano1 Blanca Lopez-Mendez1 Jesus Angulo2 Rafael Ojeda2 Pedro M. Nieto2 Manuel Martin-Lomas2 Guillermo Gimenez-Gallego1 and Jesus Jimenez-Barbero1 1 Centro de Investigaciones Madrid Spain 2 Instituto de Investigaciones Químicas CSIC Seville Spain Keywords fibroblast growth factor heparin-like hexasaccharide protein-carbohydrate complex Correspondence J. Jimenez-Barbero Centro de Investigaciones Biologicas CSIC Ramiro de Maeztu 9 28006 Madrid Spain Fax 34 915360432 Tel 34 918373112 E-mail jjbarbero@ Received 10 May 2006 revised 6 July 2006 accepted 18 August 2006 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. doi The human and mouse fibroblast growth factor FGF family consists of 18 members that share a common homologous core 1-3 . FGF-1 and -2 properties have often been considered paradigmatic for the whole family. Proteins including FGF-like domains have also been detected in invertebrates 2 . FGFs are involved in a wide variety of physiological processes besides the control of cell .

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