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Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/37507
Título

Backbone dynamics of a biologically active human FGF-1 monomer, complexed to a hexasaccharide heparin-analogue, by 15N NMR relaxation methods

AutorCanales, Ángeles ; Fayos, Rosa ; Angulo, Jesús ; Ojeda, Rafael; Martín-Pastor, Manuel; Nieto, Pedro M. ; Martín-Lomas, Manuel; Lozano, R.M. ; Giménez-Gallego, Guillermo ; Jiménez-Barbero, Jesús
Palabras claveChemical shift perturbation
Fibroblast growth factors
Heparan sulfate oligosaccharides
Protein-carbohydrate interactions
Relaxation analysis
Fecha de publicación2006
EditorSpringer
CitaciónJournal of Biomolecular NMR 35(4): 225-239 (2006)
ResumenThe binding site and backbone dynamics of a bioactive complex formed by the acidic fibroblast growth factor (FGF-1) and a specifically designed heparin hexasaccharide has been investigated by HSQC and relaxation NMR methods. The comparison of the relaxation data for the free and bound states has allowed showing that the complex is monomeric, and still induces mutagenesis, and that the protein backbone presents reduced motion in different timescale in its bound state, except in certain points that are involved in the interaction with the fibroblast growth factor receptor (FGFR).
Descripción15 páginas, 7 figuras, 1 tabla.
Versión del editorhttp://dx.doi.org/10.1007/s10858-006-9024-y
URIhttp://hdl.handle.net/10261/37507
DOI10.1007/s10858-006-9024-y
ISSN0925-2738
Referencias16937240
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