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Statements

Subject Item
n2:RIV%2F00216224%3A14310%2F08%3A00024972%21RIV10-MSM-14310___
rdf:type
n12:Vysledek skos:Concept
dcterms: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. 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.
dcterms:title
Studying the binding properties of BclA lectin - experiment and modeling Studying the binding properties of BclA lectin - experiment and modeling
skos:prefLabel
Studying the binding properties of BclA lectin - experiment and modeling Studying the binding properties of BclA lectin - experiment and modeling
skos:notation
RIV/00216224:14310/08:00024972!RIV10-MSM-14310___
n3:aktivita
n4:P n4:Z
n3:aktivity
P(GA303/06/0570), Z(MSM0021622413)
n3:dodaniDat
n17:2010
n3:domaciTvurceVysledku
n5:9309616 n5:7678037 Imberty, Anne n5:4347374 n5:3543331 n5:5522064
n3:druhVysledku
n9:D
n3:duvernostUdaju
n19:S
n3:entitaPredkladatele
n6:predkladatel
n3:idSjednocenehoVysledku
398206
n3:idVysledku
RIV/00216224:14310/08:00024972
n3:jazykVysledku
n14:eng
n3:klicovaSlova
lectins; molecular modeling; isothermal titration calorimetry; docking
n3:klicoveSlovo
n7:isothermal%20titration%20calorimetry n7:lectins n7:molecular%20modeling n7:docking
n3:kontrolniKodProRIV
[BD50ACDF0E3B]
n3:mistoKonaniAkce
Athens
n3:mistoVydani
OXFORD
n3:nazevZdroje
FEBS Journal
n3:obor
n10:CE
n3:pocetDomacichTvurcuVysledku
6
n3:pocetTvurcuVysledku
7
n3:projekt
n8:GA303%2F06%2F0570
n3:rokUplatneniVysledku
n17:2008
n3:tvurceVysledku
Wimmerová, Michaela Malinovská, Lenka Kříž, Zdeněk Adam, Jan Koča, Jaroslav Lameignere, Emily Imberty, Anne
n3:typAkce
n21:WRD
n3:wos
000256633300472
n3:zahajeniAkce
2008-01-01+01:00
n3:zamer
n18:MSM0021622413
s:issn
1742-464X
s:numberOfPages
1
n15:hasPublisher
BLACKWELL PUBLISHING
n16:organizacniJednotka
14310