Structural basis of high-affinity glycan recognition by bacterial and fungal lectins
| Authors | |
|---|---|
| Year of publication | 2005 |
| Type | Article in Periodical |
| Magazine / Source | Current Opinion in Structural Biology |
| MU Faculty or unit | |
| 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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