About: Engineering the Pseudomonas aeruginosa II lectin: designing mutants with changed affinity and specificity

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About: Engineering the Pseudomonas aeruginosa II lectin: designing mutants with changed affinity and specificity Goto Sponge NotDistinct Permalink

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

Attributes	Values
rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
rdfs:seeAlso	http://link.springer.com/article/10.1007%2Fs10822-014-9774-7
Description	This article focuses on designing mutations of the PA-IIL lectin from Pseudomonas aeruginosa that lead to change in specificity. Following the previous results revealing the importance of the amino acid triad 22–23–24 (so-called specificity-binding loop), saturation in silico mutagenesis was performed, with the intent of finding mutations that increase the lectin’s affinity and modify its specificity. For that purpose, a combination of docking, molecular dynamics and binding free energy calculation was used. The combination of methods revealed mutations that changed the performance of the wild-type lectin and its mutants to their preferred partners. The mutation at position 22 resulted in 85 % in inactivation of the binding site, and the mutation at 23 did not have strong effects thanks to the side chain being pointed away from the binding site. This article focuses on designing mutations of the PA-IIL lectin from Pseudomonas aeruginosa that lead to change in specificity. Following the previous results revealing the importance of the amino acid triad 22–23–24 (so-called specificity-binding loop), saturation in silico mutagenesis was performed, with the intent of finding mutations that increase the lectin’s affinity and modify its specificity. For that purpose, a combination of docking, molecular dynamics and binding free energy calculation was used. The combination of methods revealed mutations that changed the performance of the wild-type lectin and its mutants to their preferred partners. The mutation at position 22 resulted in 85 % in inactivation of the binding site, and the mutation at 23 did not have strong effects thanks to the side chain being pointed away from the binding site. (en)
Title	Engineering the Pseudomonas aeruginosa II lectin: designing mutants with changed affinity and specificity Engineering the Pseudomonas aeruginosa II lectin: designing mutants with changed affinity and specificity (en)
skos:prefLabel	Engineering the Pseudomonas aeruginosa II lectin: designing mutants with changed affinity and specificity Engineering the Pseudomonas aeruginosa II lectin: designing mutants with changed affinity and specificity (en)
skos:notation	RIV/00216224:14740/14:00073859!RIV15-MSM-14740___
http://linked.open...avai/riv/aktivita	P S
http://linked.open...avai/riv/aktivity	P(ED1.1.00/02.0068), P(GA13-25401S), P(LH13055), S
http://linked.open...iv/cisloPeriodika	9
http://linked.open...vai/riv/dodaniDat	2015
http://linked.open...aciTvurceVysledku	Adam, Jan Koča, Jaroslav Wimmerová, Michaela Mrázková, Jana Kříž, Zdeněk Chatzipavlou, Thomais Zotos, Petros
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Masarykova univerzita / Středoevropský technologický institut
http://linked.open...dnocenehoVysledku	14640
http://linked.open...ai/riv/idVysledku	RIV/00216224:14740/14:00073859
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	Lectin; Carbohydrate; Mutagenesis; Docking; Molecular dynamics (en)
http://linked.open.../riv/klicoveSlovo	Molecular dynamics Docking Lectin Mutagenesis Carbohydrate
http://linked.open...odStatuVydavatele	CH - Švýcarská konfederace
http://linked.open...ontrolniKodProRIV	[F2AAB0A820E1]
http://linked.open...i/riv/nazevZdroje	Journal of Computer-Aided Molecular Design
http://linked.open...in/vavai/riv/obor	CE
http://linked.open...ichTvurcuVysledku	7 (xsd:int)
http://linked.open...cetTvurcuVysledku	7 (xsd:int)
http://linked.open...vavai/riv/projekt	Study of proteins from pathogens involved in host organism recognition Multidisciplinary Approach to Drug Design - Inhibition of Carbohydrate Acting Proteins Central european institute of technology
http://linked.open...UplatneniVysledku	2014
http://linked.open...v/svazekPeriodika	28
http://linked.open...iv/tvurceVysledku	Adam, Jan Koča, Jaroslav Mrázková, Jana Wimmerová, Michaela Kříž, Zdeněk Chatzipavlou, Thomais Zotos, Petros
http://linked.open...ain/vavai/riv/wos	000342439000006
issn	0920-654X
number of pages	10 (xsd:int)
http://bibframe.org/vocab/doi	10.1007/s10822-014-9774-7
http://localhost/t...ganizacniJednotka	14740

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