| Literature DB >> 16622409 |
Antonio Greco1, Jason G S Ho, Shuang-Jun Lin, Monica M Palcic, Maja Rupnik, Kenneth K-S Ng.
Abstract
Clostridium difficile TcdA is a large toxin that binds carbohydrates on intestinal epithelial cells. A 2-A resolution cocrystal structure reveals two molecules of alpha-Gal-(1,3)-beta-Gal-(1,4)-beta-GlcNAcO(CH(2))(8)CO(2)CH(3) 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.Entities:
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Year: 2006 PMID： 16622409 DOI： 10.1038/nsmb1084
Source DB: PubMed Journal: Nat Struct Mol Biol ISSN： 1545-9985 Impact factor: 15.369