About: Studying the binding properties of BclA lectin

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An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
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. (en)
Title	Studying the binding properties of BclA lectin - experiment and modeling Studying the binding properties of BclA lectin - experiment and modeling (en)
skos:prefLabel	Studying the binding properties of BclA lectin - experiment and modeling Studying the binding properties of BclA lectin - experiment and modeling (en)
skos:notation	RIV/00216224:14310/08:00024972!RIV10-MSM-14310___
http://linked.open...avai/riv/aktivita	P Z
http://linked.open...avai/riv/aktivity	P(GA303/06/0570), Z(MSM0021622413)
http://linked.open...vai/riv/dodaniDat	2010
http://linked.open...aciTvurceVysledku	Adam, Jan Malinovská, Lenka Koča, Jaroslav Wimmerová, Michaela Kříž, Zdeněk Imberty, Anne
http://linked.open.../riv/druhVysledku	D - Článek ve sborníku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Masarykova univerzita / Přírodovědecká fakulta
http://linked.open...dnocenehoVysledku	398206
http://linked.open...ai/riv/idVysledku	RIV/00216224:14310/08:00024972
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	lectins; molecular modeling; isothermal titration calorimetry; docking (en)
http://linked.open.../riv/klicoveSlovo	lectins docking molecular modeling isothermal titration calorimetry
http://linked.open...ontrolniKodProRIV	[BD50ACDF0E3B]
http://linked.open...v/mistoKonaniAkce	Athens
http://linked.open...i/riv/mistoVydani	OXFORD
http://linked.open...i/riv/nazevZdroje	FEBS Journal
http://linked.open...in/vavai/riv/obor	CE
http://linked.open...ichTvurcuVysledku	6 (xsd:int)
http://linked.open...cetTvurcuVysledku	7 (xsd:int)
http://linked.open...vavai/riv/projekt	Structure-function studies on lectins and adhesins from microbial patogens
http://linked.open...UplatneniVysledku	2008
http://linked.open...iv/tvurceVysledku	Adam, Jan Imberty, Anne Koča, Jaroslav Malinovská, Lenka Wimmerová, Michaela Kříž, Zdeněk Lameignere, Emily
http://linked.open...vavai/riv/typAkce	WRD - Světová
http://linked.open...ain/vavai/riv/wos	000256633300472
http://linked.open.../riv/zahajeniAkce	2008-01-01 (xsd:date)
http://linked.open...n/vavai/riv/zamer	Proteiny v metabolismu a při interakci organismů s prostředím
issn	1742-464X
number of pages	1 (xsd:int)
http://purl.org/ne...btex#hasPublisher	BLACKWELL PUBLISHING
http://localhost/t...ganizacniJednotka	14310
is http://linked.open...avai/riv/vysledek of	Studying the binding properties of BclA lectin - experiment and modeling Studying the binding properties of BclA lectin - experiment and modeling Studying the binding properties of BclA lectin - experiment and modeling Studying the binding properties of BclA lectin - experiment and modeling

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