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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