Abstract:
: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).
journal_name
J Biomol NMRjournal_title
Journal of biomolecular NMRauthors
Canales-Mayordomo A,Fayos R,Angulo J,Ojeda R,Martín-Pastor M,Nieto PM,Martín-Lomas M,Lozano R,Giménez-Gallego G,Jiménez-Barbero Jdoi
10.1007/s10858-006-9024-ysubject
Has Abstractpub_date
2006-08-01 00:00:00pages
225-39issue
4eissn
0925-2738issn
1573-5001journal_volume
35pub_type
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