It is suggested that the interactions between the hydrophobic C-H groups of carbohydrate residues and the pi-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/pi interactions are involved in the actual binding events.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.2174/0929866023408751 | DOI Listing |
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!