The importance of CH/pi interactions to the function of carbohydrate binding proteins.
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.
Muraki
Michiro
M
Biological Information Research Center, National Institute of Advanced Industrial Science and Technology, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan. muraki@aist.go.jp
D023181:Antimicrobial Cationic Peptides; D002240:Carbohydrate Sequence; D002241:Carbohydrates / Q000737:chemistry*; D004583:Electrons; D006801:Humans; D037102:Lectins / Q000737:chemistry; D008024:Ligands; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009113:Muramidase / Q000737:chemistry; D037121:Plant Lectins / Q000737:chemistry; D011485:Protein Binding; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D013997:Time Factors
D023181:Antimicrobial Cationic Peptides; D002241:Carbohydrates; D037102:Lectins; D008024:Ligands; D037121:Plant Lectins; C045875:hevein; D009113:Muramidase