Carbohydrate recognition by Clostridium difficile toxin A

被引：112

作者：

Greco, A

Ho, JGS

Lin, SJ

Palcic, MM

Rupnik, M

Ng, KKS ^{[1
]}

机构：

[1] Univ Calgary, Alberta Ingenu Ctr Carbohydrate Sci, Calgary, AB T2N 1N4, Canada

[2] Univ Calgary, Dept Biol Sci, Calgary, AB T2N 1N4, Canada

[3] Inst Publ Hlth, Maribor, Slovenia

[4] Univ Alberta, Dept Chem, Edmonton, AB, Canada

[5] Carlsberg Lab, Valby, Denmark

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2006年 / 13卷 / 05期

基金：

美国国家科学基金会; 加拿大健康研究院; 美国国家卫生研究院;

关键词：

D O I：

10.1038/nsmb1084

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：

Clostridium difficile TcdA is a large toxin that binds carbohydrates on intestinal epithelial cells. A 2-angstrom resolution cocrystal structure reveals two molecules of alpha-Gal-(1,3)-beta-Gal-(1,4)-beta-GlcNAcO(CH2)(8)CO2CH3 binding in an extended conformation to TcdA. Residues forming key contacts with the trisaccharides are conserved in all seven putative binding sites in TcdA, suggesting a mode of multivalent binding that may be exploited for the rational design of novel therapeutics.

引用

页码：460 / 461

页数：2

共 16 条

[11] Molecular mimicry in the recognition of glycosphingolipids by Gal alpha 3Gal beta 4GlcNAc beta-binding Clostridium difficile toxin A, human natural anti alpha-galactosyl IgG and the monoclonal antibody Gal-13: Characterization of a binding-active human glycosphingolipid, non-identical with the animal receptor [J].