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; Albert M. WU; Michaela WIMMEROVÁ; Corrine HOULES; Edward MITCHELL; Dvora SUDAKEVITZ a Nechama GILBOA-GARBER

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

Označené pro přenos do RIV

Ano

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  - CONF
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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