"[BD50ACDF0E3B]" . . . . . . . "Wimmerov\u00E1, Michaela" . . . "Imberty, Anne" . "000256633300472" . . "Malinovsk\u00E1, Lenka" . . "K\u0159\u00ED\u017E, Zden\u011Bk" . "RIV/00216224:14310/08:00024972!RIV10-MSM-14310___" . . "398206" . "Studying the binding properties of BclA lectin - experiment and modeling"@en . . . "BLACKWELL PUBLISHING" . "Adam, Jan" . "14310" . "Studying the binding properties of BclA lectin - experiment and modeling" . . "RIV/00216224:14310/08:00024972" . "P(GA303/06/0570), Z(MSM0021622413)" . . . "Ko\u010Da, Jaroslav" . "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."@en . . "2008-01-01+01:00"^^ . "lectins; molecular modeling; isothermal titration calorimetry; docking"@en . "Athens" . . "Lameignere, Emily" . . . "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." . "1742-464X" . . . "OXFORD" . "Studying the binding properties of BclA lectin - experiment and modeling"@en . "1"^^ . "Studying the binding properties of BclA lectin - experiment and modeling" . "6"^^ . "7"^^ . "FEBS Journal" . "Imberty, Anne" . .