TY - JOUR
T1 - Backbone dynamics of a biologically active human FGF-1 monomer, complexed to a hexasaccharide heparin-analogue, by N NMR relaxation methods
AU - Canales-Mayordomo, A.
AU - Fayos, R.
AU - Lozano, R.
AU - Giménez-Gallego, G.
AU - Jiménez-Barbero, J.
AU - Angulo, J.
AU - Ojeda, R.
AU - Nieto, P.M.
AU - Martín-Lomas, M.
AU - Martín-Pastor, M.
PY - 2006/8/1
Y1 - 2006/8/1
N2 - The 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).
AB - The 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).
UR - http://www.scopus.com/inward/record.url?scp=33747885811&partnerID=8YFLogxK
U2 - 10.1007/s10858-006-9024-y
DO - 10.1007/s10858-006-9024-y
M3 - Article
AN - SCOPUS:33747885811
VL - 35
SP - 225
EP - 239
JO - Journal of Biomolecular NMR
JF - Journal of Biomolecular NMR
SN - 0925-2738
IS - 4
ER -