Structural and thermodynamical characterisation of interaction between a pseudomonas lectin and monosaccharides

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F03%3A00008865" target="_blank" >RIV/00216224:14310/03:00008865 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Structural and thermodynamical characterisation of interaction between a pseudomonas lectin and monosaccharides

Popis výsledku v původním jazyce

Pseudomonas aeruginosa galactose- and fucose-binding (PA-IL and PA-IIL) lectins contribute to the virulence of this pathogenic bacterium, which is a major cause of morbidity and mortality in cystic fibrosis patients. The crystal structure of PA-IIL complexed with fucose has been solved at 1.3 A and further refined at 1 Ĺ resolution. Additional experiments have been performed in order to understand the molecular basis of both specificity and affinity of PA-IIL for monosaccharides. Crystals have been obtained for the complex between PA-ILL and b-Me-D-arabinopyranoside and the structure has been solved at 1.8 A resolution. PA-IIL exhibits unusually high specificity to fucose, which can be related to the presence of two calcium ions in the site. Isothermaltitration microcalorimetry (ITC) experiments were performed in order to characterize the thermodynamic parameters of the interaction since this method has been proven to be well adapted to the study of protein/carbohydrate interactions.

Název v anglickém jazyce

Structural and thermodynamical characterisation of interaction between a pseudomonas lectin and monosaccharides

Popis výsledku anglicky

Pseudomonas aeruginosa galactose- and fucose-binding (PA-IL and PA-IIL) lectins contribute to the virulence of this pathogenic bacterium, which is a major cause of morbidity and mortality in cystic fibrosis patients. The crystal structure of PA-IIL complexed with fucose has been solved at 1.3 A and further refined at 1 Ĺ resolution. Additional experiments have been performed in order to understand the molecular basis of both specificity and affinity of PA-IIL for monosaccharides. Crystals have been obtained for the complex between PA-ILL and b-Me-D-arabinopyranoside and the structure has been solved at 1.8 A resolution. PA-IIL exhibits unusually high specificity to fucose, which can be related to the presence of two calcium ions in the site. Isothermaltitration microcalorimetry (ITC) experiments were performed in order to characterize the thermodynamic parameters of the interaction since this method has been proven to be well adapted to the study of protein/carbohydrate interactions.

Druh

D - Stať ve sborníku

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/LN00A016" target="_blank" >LN00A016: BIOMOLEKULÁRNÍ CENTRUM</a><br>

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

12th European Carbohydrate Symposium

ISBN

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ISSN

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e-ISSN

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Počet stran výsledku

1

Strana od-do

390

Název nakladatele

CERMAV-CNRS

Místo vydání

Grenoble, France

Místo konání akce

Grenoble, France

Datum konání akce

1. 1. 2003

Typ akce podle státní příslušnosti

WRD - Celosvětová akce

Kód UT WoS článku

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