Pseudomonas aeruginosa lectin PA-IIL displays a novel carbohydrate recognition mode: Structural analysis of complexes with fucose and oligosaccharides.
| Autoři | |
|---|---|
| Rok publikování | 2003 |
| Druh | Článek ve sborníku |
| Konference | XVII International Symposium on Glycoconjugates |
| Fakulta / Pracoviště MU | |
| Citace | |
| Obor | Biochemie |
| Klíčová slova | Pseudomonas aeruginosa; lectin; crystal structure; cystic fibrosis |
| Popis | Pseudomonas aeruginosa galactose (PA-IL) and fucose-binding (PA-IIL) lectins contribute to the virulence of this pathogenic bacterium. Determination of the crystal structure of PA-IIL complexed with fucose demonstrates a tetrameric structure. Each monomer displays a nine-stranded antiparallel b-sandwich arrangement and contains two calcium cations in one binding site. In each monomer, the calcium binding pocket is formed by two b-strand-connecting loops together with the C-terminal extremity of the adjacent monomer. The fucose-lectin interaction is mediated by the two calcium ions. Such a binding mode is unique in carbohydrate-protein recognition. Three of the fucose hydroxyl groups participate in the coordination spheres of the two calcium ions. Experimental binding studies together with theoretical docking of fucose-containing oligosaccharides are consistent with the assumptions that antigens of the Lewis A series might be the preferred ligands of this lectin. Precise knowledge of the lectin binding site, should allow for a better design of new antiadhesive glycoderived or glycomimetic drugs. |
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