Pseudomonas aeruginosa lectin PA-IIL displays a novel
carbohydrate recognition mode: Structural analysis of complexes
with fucose and oligosaccharides.

D 2003

Pseudomonas aeruginosa lectin PA-IIL displays a novel carbohydrate recognition mode: Structural analysis of complexes with fucose and oligosaccharides.

IMBERTY, Anne, Albert M. WU, Michaela WIMMEROVÁ, Corrine HOULES, Edward MITCHELL et. al.

Základní údaje

Originální název

Pseudomonas aeruginosa lectin PA-IIL displays a novel carbohydrate recognition mode: Structural analysis of complexes with fucose and oligosaccharides.

Autoři

IMBERTY, Anne (250 Francie), Albert M. WU (158 Tchaj-wan), Michaela WIMMEROVÁ (203 Česká republika, garant), Corrine HOULES (250 Francie), Edward MITCHELL (250 Francie), Dvora SUDAKEVITZ (376 Izrael) a Nechama GILBOA-GARBER (376 Izrael)

Vydání

Bangalore, Indie, XVII International Symposium on Glycoconjugates, s. 34-34, 2003

Nakladatel

Další údaje

Jazyk

angličtina

Typ výsledku

Stať ve sborníku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Indie

Utajení

není předmětem státního či obchodního tajemství

Kód RIV

RIV/00216224:14310/03:00008867

Organizační jednotka

Přírodovědecká fakulta

Klíčová slova anglicky

Pseudomonas aeruginosa; lectin; crystal structure; cystic fibrosis

Štítky

Crystal Structure, cystic fibrosis, lectin, Pseudomonas aeruginosa

Příznaky

Mezinárodní význam

Změněno: 15. 11. 2006 11:39, prof. RNDr. Michaela Wimmerová, Ph.D.

Anotace

V originále

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.

Návaznosti

LN00A016, projekt VaV

Název: BIOMOLEKULÁRNÍ CENTRUM

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Biomolekulární centrum

Citovat

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.

@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.

Podrobný výpis o publikaci