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

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Authors

IMBERTY Anne MITCHELL Edward P. WIMMEROVÁ Michaela

Year of publication 2005
Type Article in Periodical
Magazine / Source Current Opinion in Structural Biology
MU Faculty or unit

Faculty of Science

Citation
Field Biochemistry
Keywords lectin; pathogen; crystal structure; recognition
Description 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
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