Abstract
It is suggested that the interactions between the hydrophobic C-H groups of carbohydrate residues and the p-electron systems of aromatic amino-acid residues play an important role in the ligand-recognition function of carbohydrate-binding proteins. This review focuses on our recent structural and functional studies of human lysozyme and hevein-domain type lectins (wheat-germ agglutinin and Ac-AMP2) aimed at understanding how CH / π interactions are involved in the actual binding events.
Keywords: interaction, carbohydrate binding protein, cbp interaction