Characterization of the galectin-1 carbohydrate recognition domain in terms of solvent occupancy.

S. DI LELLA; M. A. MARTI; R.M.S. ALVAREZ; D.A. ESTRIN; J.C. DIAZ RICCI

JOURNAL OF PHYSICAL CHEMISTRY B

American Chemical Society

Año: 2007 vol. 111 p. 7360 - 7366

1089-5647

Human galectin-1, a galactosil-terminal sugar binding soluble protein, is a potent multifunctional effectorthat participates in specific protein-carbohydrate and protein-protein interactions. Recent studies revealedthat it plays a key role as a modulator of cellular differentiation and immunological response. In this work,we have investigated the solvation properties of the carbohydrate recognition domain of Gal-1 by means ofmolecular dynamics simulations. Water sites (ws) were identified in terms of radial and angular distributionfunctions, and properties such as water residence times, interaction energies, and free-energy contributionswere evaluated for those sites. Our results allowed us to correlate the thermodynamic properties of the wsand their binding pattern with the N-acetilgalactoside ligand. These results let us further infer that the watermolecules located at the ws, which exhibit much more favorable binding, are the ones replaced by -OHgroups of the sugar.