Muraki Michiro
Biological Information Research Center, National Institute of Advanced Industrial Science and Technology, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan.
Protein Pept Lett. 2002 Jun;9(3):195-209. doi: 10.2174/0929866023408751.
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.
有人提出,碳水化合物残基的疏水C-H基团与芳香族氨基酸残基的π电子系统之间的相互作用在碳水化合物结合蛋白的配体识别功能中起重要作用。本综述重点关注我们最近对人溶菌酶和橡胶素结构域型凝集素(麦胚凝集素和Ac-AMP2)的结构和功能研究,旨在了解CH/π相互作用是如何参与实际结合事件的。