PROTEIN CARBOHYDRATE INTERACTIONS

被引：42

作者：

BOURNE, Y ^{[1
]}

VANTILBEURGH, H ^{[1
]}

CAMBILLAU, C ^{[1
]}

机构：

[1] CNRS,F-13274 MARSEILLE 2,FRANCE

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 1993年 / 3卷 / 05期

关键词：

D O I：

10.1016/0959-440X(93)90050-U

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：

X-ray structures of protein-carbohydrate complexes reported this year confirm well established rules of protein-carbohydrate interactions: stabilization through a network of hydrogen bonds often involving water molecules, and hydrophobic interactions. The importance of the latter interactions have been tested in a few cases by site-directed mutagenesis experiments. In contrast, new insights have emerged regarding biologically and catalytically relevant carbohydrate-metal interactions. Carbohydrate flexibility and ring opening play crucial roles in catalysis, as demonstrated by the structures of neuraminidase and xylose isomerase.

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页码：681 / 686

页数：6

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