期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 13, 期 5, 页码 460-461出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb1084
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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.
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