Structural basis of high-affinity glycan recognition by bacterial and fungal lectins

被引：77

作者：

Imberty, A

Mitchell, EP

Wimmerová, M

机构：

[1] Univ Grenoble 1, CNRS, CERMAV, F-38041 Grenoble, France

[2] European Synchrotron Radiat Facil, Expt Div, F-38043 Grenoble, France

[3] Masaryk Univ, Natl Ctr Biomol Res, CS-61137 Brno, Czech Republic

[4] Masaryk Univ, Dept Biochem, CS-61137 Brno, Czech Republic

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2005年 / 15卷 / 05期

关键词：

D O I：

10.1016/j.sbi.2005.08.003

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：

The structural diversity of bacterial and fungal lectins has been highlighted during the past few years. Some of the new structures reproduce folds previously observed in plants or mammals, but many constitute new folds that have never been observed before, either at all or not with a lectin function, testifying to the increasing diversity. The novelty of the new structures is greater at the level of the sugar-binding sites, with some bacterial lectins displaying unusually high affinity for oligosaccharides and even monosaccharides. Analysis of the thermodynamic contributions to the energy of binding gives clues to the strategies used by bacteria to recognise and attach to their host.

引用

收藏

页码：525 / 534

页数：10

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