Studying the binding properties of BclA lectin - experiment and modeling

Result code in 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>

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

Studying the binding properties of BclA lectin - experiment and modeling

Original language description

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

Czech name

Studying the binding properties of BclA lectin - experiment and modeling

Czech description

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

Type

D - Article in proceedings

CEP classification

CE - Biochemistry

OECD FORD branch

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Project

<a href="/en/project/GA303%2F06%2F0570" target="_blank" >GA303/06/0570: Structure-function studies on lectins and adhesins from microbial patogens</a><br>

Continuities

Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2008

Confidentiality

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

Article name in the collection

FEBS Journal

ISBN

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ISSN

1742-464X

e-ISSN

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Number of pages

1

Pages from-to

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Publisher name

BLACKWELL PUBLISHING

Place of publication

OXFORD

Event location

Athens

Event date

Jan 1, 2008

Type of event by nationality

WRD - Celosvětová akce

UT code for WoS article

000256633300472