Cañada Vicinay, Francisco Javier
91 837 3112 Extension: 4374/4373
The nuclear magnetic resonance (NMR) group, under leadership of Prof. Jiménez Barbero and Prof. J. Cañada is interested in the development of general methodological aspects of the NMR techniques and, particularly, in their applications to the study of the conformation and dynamics of the molecular recognition processes. During the last few years we have determined the solution 3D structure of different proteins using a protocol based on NMR spectroscopy, assisted by molecular mechanics and dynamics calculations.
This methodology has been applied to different carbohydrate molecular complexes of wild type and mutant lectins, glycosidases, and to the elucidation of the structure of other protein receptors of biomedical interest. We have investigated protein complexes with natural ligands and with synthetically modified analogues.
We have also investigated the structural characteristics, both from the conformational and dynamical point of view of different biologically relevant oligo and polysacharides also using NMR and molecular dynamics. In particular, we have paid attention to the physical-chemical origin of the interaction between carbohydrates and proteins, with special emphasis in the relative role of sugar-aromatic stacking interactions.
Natural abundance as well as labeled ligands and proteins (13C, 15N) have been used for these studies.
Thanks to the collaboration with several research groups throughout the world, some studied systems include galectins, in which we are deeply involved, through a long standing collaboration with Prof. HJ Gabius, hevein domains, ricin-B, viscumin, lactase, E. coli beta-galactosidase, Streptomyces Sp. beta-glucosidase, ribonuclease B, DC-SIGN, acidic fibroblast growth factor, cholera toxin B, HexS1 homeodomain, glycomimetics, C- and S-glycosyl compounds, aminoglycosides, carbohydrate antigens, bacterial and fungal polysaccharides, etc.
This last research line overlaps with a, still alive, old one of the group, aimed at establishing the structural basis of the inhibition/activation of fibroblast growth factor and its receptor, a protein deeply involved in important pathologies, and at designing inhibitors of its mitogenic activity (with Prof. Giménez-Gallego).
These studies require relatively simple studies of cell biology sometimes. We are also interested in the determination of the enzyme UDP-glucose pyrophosphorylase, a key component of the pneumococcal cell capsule in all the known strains of this bacterium. The group collaborates with numerous Spanish and foreign research laboratories in numerous other projects not directly related with its main research goals.