| IMBERTY, Anne, Albert M. WU, Michaela WIMMEROVÁ, Corrine HOULES, Edward MITCHELL, Dvora SUDAKEVITZ a Nechama GILBOA-GARBER. Pseudomonas aeruginosa lectin PA-IIL displays a novel carbohydrate recognition mode: Structural analysis of complexes with fucose and oligosaccharides. In XVII International Symposium on Glycoconjugates. Bangalore, Indie: AS, 2003, s. 34. |
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@inproceedings{488306,
author = {Imberty, Anne and Wu, Albert M. and Wimmerová, Michaela and Houles, Corrine and Mitchell, Edward and Sudakevitz, Dvora and GilboaandGarber, Nechama},
address = {Bangalore, Indie},
booktitle = {XVII International Symposium on Glycoconjugates},
keywords = {Pseudomonas aeruginosa; lectin; crystal structure; cystic fibrosis},
language = {eng},
location = {Bangalore, Indie},
pages = {34-34},
publisher = {AS},
title = {Pseudomonas aeruginosa lectin PA-IIL displays a novel carbohydrate recognition mode: Structural analysis of complexes with fucose and oligosaccharides.},
year = {2003}
}
TY - JOUR
ID - 488306
AU - Imberty, Anne - Wu, Albert M. - Wimmerová, Michaela - Houles, Corrine - Mitchell, Edward - Sudakevitz, Dvora - Gilboa-Garber, Nechama
PY - 2003
TI - Pseudomonas aeruginosa lectin PA-IIL displays a novel carbohydrate recognition mode: Structural analysis of complexes with fucose and oligosaccharides.
PB - AS
CY - Bangalore, Indie
KW - Pseudomonas aeruginosa
KW - lectin
KW - crystal structure
KW - cystic fibrosis
N2 - 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.
ER -
IMBERTY, Anne, Albert M. WU, Michaela WIMMEROVÁ, Corrine HOULES, Edward MITCHELL, Dvora SUDAKEVITZ a Nechama GILBOA-GARBER. Pseudomonas aeruginosa lectin PA-IIL displays a novel carbohydrate recognition mode: Structural analysis of complexes with fucose and oligosaccharides. In \textit{XVII International Symposium on Glycoconjugates}. Bangalore, Indie: AS, 2003, s.~34.
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