New structural insights into lectin-type proteins of the immune system

被引：45

作者：

Kogelberg, H ^{[1
]}

Feizi, T ^{[1
]}

机构：

[1] Univ London Imperial Coll Sci Technol & Med, Northwick Pk Inst Med Res, Fac Med, Glycosci Lab, Harrow HA1 3UJ, Middx, England

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2001年 / 11卷 / 05期

基金：

英国医学研究理事会;

关键词：

D O I：

10.1016/S0959-440X(00)00259-1

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：

New structural data have emerged for the ligand-binding sites of C-type lectin domains and C-type lectin-like domains of receptors of the immune system. These include binding sites for oligosaccharide or polypeptide ligands, or both oligosaccharide and polypeptide ligands. The structural basis for the binding of a lectin domain of the beta -trefoil family to different sulfo-oligosaccharide sequences has been revealed. Lectin activity has been documented for a beta/alpha, TIM barrel fold that does not have the chitinase activity of the prototype enzyme with this fold.

引用

收藏

页码：635 / 643

页数：9

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