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  • Title: Probing hydrogen-bonding interactions of bovine heart galectin-1 and methyl beta-lactoside by use of engineered ligands.
    Author: Solís D, Jiménez-Barbero J, Martín-Lomas M, Díaz-Mauriño T.
    Journal: Eur J Biochem; 1994 Jul 01; 223(1):107-14. PubMed ID: 8033884.
    Abstract:
    The binding of different synthetic monodeoxy, O-methyl and fluorodeoxy derivatives of methyl beta-lactoside to galectin-1 from bovine heart has been studied to probe the role of hydrogen bonding in the recognition and binding. The energetic contributions of the hydroxyl groups of methyl beta-lactoside directly involved in the interaction have been estimated and the nature of the protein residues involved has been predicted on the basis of the free energy data. Interpretations of the results have been sustained by molecular modeling of the three-dimensional structure of the sugars in solution. One side of the disaccharide molecule is not involved (HO-6 and HO-2') or only marginally involved (HO-3') in hydrogen bonding. Moreover, O-methylation at these positions causes an enhancement of the binding, suggesting favourable interactions of the methyl groups which may come into contact with hydrophobic residues at the periphery of the combining site. Hydrogen-bonding interactions are almost exclusively restricted to the other side of the molecule: the C-4' and C-6' hydroxyl groups act as donors of the strongest hydrogen bonds to charged groups of the lectin, while the C-3 hydroxyl group participates in a strong hydrogen bond with a neutral group. The results also suggest that the N-acetyl NH group in N-acetyllactosamine, as well as the hydroxyl group at position C-2 in methyl beta-lactoside, are involved in a polar interaction with neutral groups of the combining site. This hydrogen-bonding pattern contrasts markedly with that previously reported for the two galactose-specific Ricinus communis lectins. The recognition of different epitopes of the same basic structure underlies the differences in the oligosaccharide-binding specificities of galectin-1 and the R. communis lectins.
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