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

Kód výsledku v IS VaVaI

RIV/00216224:14310/03:00008867 - isvavai.cz

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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 th

Název v anglickém jazyce

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

Popis výsledku anglicky

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 th

Druh

D - Stať ve sborníku

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

LN00A016: BIOMOLEKULÁRNÍ CENTRUM

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2003

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název statě ve sborníku

XVII International Symposium on Glycoconjugates

ISBN

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ISSN

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e-ISSN

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Počet stran výsledku

1

Strana od-do

34

Název nakladatele

AS

Místo vydání

Bangalore, Indie

Místo konání akce

Bangalore, Indie

Datum konání akce

1. 1. 2003

Typ akce podle státní příslušnosti

WRD - Celosvětová akce

Kód UT WoS článku

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