Studying the binding properties of BclA lectin - experiment and modeling

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F08%3A00024972" target="_blank" >RIV/00216224:14310/08:00024972 - 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

Studying the binding properties of BclA lectin - experiment and modeling

Popis výsledku v původním jazyce

Burkholderia cenocepacia is a ubiquitous bacterium that can act as opportunistic human pathogen, responsible for lethal complications in cystic fibrosis patients. The genome of the bacterium contains several lectin- like sequences that are related to previously characterized fucose-preferring lectin PAIIL from Pseudomonas aeruginosa . BclA is a lectin from B.cenocepacia that shares the unique sugar binding mode common to PAIIL family lectins. Molecular docking was performed using the AUTODOCK and DOCK software. The AMBER package was used for molecular dynamics simulations. Enzyme linked lectin assay, surface plasmon resonance and isothermal titration calorimetry was used to determine the binding properties experimentally.Experiments determined that BclA prefers mannose to fucose as the binding partner. Despite the sequence similarity, BclA adopts dimeric form, as opposed to tetrameric PAIIL, possible consequence of the presence of an extra loop. Docking experiments combined with molecu

Název v anglickém jazyce

Studying the binding properties of BclA lectin - experiment and modeling

Popis výsledku anglicky

Burkholderia cenocepacia is a ubiquitous bacterium that can act as opportunistic human pathogen, responsible for lethal complications in cystic fibrosis patients. The genome of the bacterium contains several lectin- like sequences that are related to previously characterized fucose-preferring lectin PAIIL from Pseudomonas aeruginosa . BclA is a lectin from B.cenocepacia that shares the unique sugar binding mode common to PAIIL family lectins. Molecular docking was performed using the AUTODOCK and DOCK software. The AMBER package was used for molecular dynamics simulations. Enzyme linked lectin assay, surface plasmon resonance and isothermal titration calorimetry was used to determine the binding properties experimentally.Experiments determined that BclA prefers mannose to fucose as the binding partner. Despite the sequence similarity, BclA adopts dimeric form, as opposed to tetrameric PAIIL, possible consequence of the presence of an extra loop. Docking experiments combined with molecu

Druh

D - Stať ve sborníku

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/GA303%2F06%2F0570" target="_blank" >GA303/06/0570: Strukturně-funkční studie lektinů a adhezinů patogenních mikroorganismů</a><br>

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2008

Kód důvěrnosti údajů

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

Název statě ve sborníku

FEBS Journal

ISBN

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ISSN

1742-464X

e-ISSN

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Počet stran výsledku

1

Strana od-do

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Název nakladatele

BLACKWELL PUBLISHING

Místo vydání

OXFORD

Místo konání akce

Athens

Datum konání akce

1. 1. 2008

Typ akce podle státní příslušnosti

WRD - Celosvětová akce

Kód UT WoS článku

000256633300472