Stereochemical basis of high affinity of Pseudomonas aeruginosa lectin for fucose : structural and thermodynamic characterisation

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F03%3A00008871" target="_blank" >RIV/00216224:14310/03:00008871 - 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

Stereochemical basis of high affinity of Pseudomonas aeruginosa lectin for fucose : structural and thermodynamic characterisation

Popis výsledku v původním jazyce

Human pathogenic bacterium Pseudomonas aeruginosa, which is a major cause of mortality and morbidity of cystic fibrosis patients, produces fucose-binding lectin (PA-IIL) that highly contributes to the pathogen virulence.The crystal structure of PA-IIL complexed with fucose has been solved at 1.3 A [1] and 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 protein complexed with b-Me-D-arabinopyranoside and L-galactose and structures were solved by molecular replacement. Co-crystallisation of the lectin with trisaccharides of the Lea and Lex family is being in progress.Isothermal titration microcalorimetry experiments ona series of monosaccharides sharing similar stereochemical three-hydroxyl arrangement needed for recognition were performed in order to characterize the thermodynamic parameters of the carbohydrate-lectin interaction. The stereochemical

Název v anglickém jazyce

Stereochemical basis of high affinity of Pseudomonas aeruginosa lectin for fucose : structural and thermodynamic characterisation

Popis výsledku anglicky

Human pathogenic bacterium Pseudomonas aeruginosa, which is a major cause of mortality and morbidity of cystic fibrosis patients, produces fucose-binding lectin (PA-IIL) that highly contributes to the pathogen virulence.The crystal structure of PA-IIL complexed with fucose has been solved at 1.3 A [1] and 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 protein complexed with b-Me-D-arabinopyranoside and L-galactose and structures were solved by molecular replacement. Co-crystallisation of the lectin with trisaccharides of the Lea and Lex family is being in progress.Isothermal titration microcalorimetry experiments ona series of monosaccharides sharing similar stereochemical three-hydroxyl arrangement needed for recognition were performed in order to characterize the thermodynamic parameters of the carbohydrate-lectin interaction. The stereochemical

Druh

D - Stať ve sborníku

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/ME%20675" target="_blank" >ME 675: Strukturně- funkční studie lektinů bakteriálních patogenů</a><br>

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2003

Kód důvěrnosti údajů

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

Název statě ve sborníku

SET for Europe

ISBN

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ISSN

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e-ISSN

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Počet stran výsledku

1

Strana od-do

126

Název nakladatele

SET for Europe

Místo vydání

Grenoble

Místo konání akce

Grenoble, France

Datum konání akce

1. 1. 2003

Typ akce podle státní příslušnosti

EUR - Evropská akce

Kód UT WoS článku

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