INSIBIO   05451
INSTITUTO SUPERIOR DE INVESTIGACIONES BIOLOGICAS
Unidad Ejecutora - UE
artículos
Título:
Specific Intermolecular Interactions of Conserved Water with Amino Acids in the Galectin-1 Carbohydrate Recognition Domain
Autor/es:
SANTIAGO DI LELLA; ARIEL A. PETRUK; DIEGO ALONSO DE ARMIÑO; ROSA MARÍA S. ÁLVAREZ
Revista:
JOURNAL OF MOLECULAR STRUCTURE
Editorial:
ELSEVIER SCIENCE BV
Referencias:
Lugar: Amsterdam; Año: 2010 vol. 978 p. 220 - 228
ISSN:
0022-2860
Resumen:
Water molecules, rigidly associated to protein surfaces, play a key role in stabilizing
biomolecules and participating in their biological functions. Recent studies on the
solvation properties of the carbohydrate recognition domain of Galectin-1 by means of
molecular dynamic simulations have revealed the existence of several water sites which
were well correlated to both the bound water molecules observed in the crystal structure
of the protein in the free-state and to some of the hydroxyl groups of the carbohydrate
ligand observed in the crystal structure of the complexed protein. In this work, we
present a study using quantum mechanical methods (B3LYP/6-311++g(3df,3dp) //
B3LYP/6-31+g(d)) to determine the energy involved in the binding of these water
molecules to specific amino acids in the carbohydrate recognition domain of the protein.
By modeling the hydroxyl groups of the carbohydrate by methanol, the energies
associated to the local interactions between the ligand and the protein have been
evaluated by replacing specific water molecules with methanol. The values of the
binding energies have been compared to those previously obtained by the molecular
dynamic method.