The importance of CH/π interactions to the function of carbohydrate binding proteins

被引：83

作者：

Muraki, M ^{[1
]}

机构：

[1] Natl Inst Adv Inst Sci & Technol, Biol Informat Res Ctr, Tsukuba, Ibaraki 3058566, Japan

来源：

PROTEIN AND PEPTIDE LETTERS | 2002年 / 9卷 / 03期

关键词：

D O I：

10.2174/0929866023408751

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：195 / 209

页数：15

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