This HTML5 document contains 57 embedded RDF statements represented using HTML+Microdata notation.

The embedded RDF content will be recognized by any processor of HTML5 Microdata.

Namespace Prefixes

PrefixIRI
dctermshttp://purl.org/dc/terms/
n20http://localhost/temp/predkladatel/
n13http://linked.opendata.cz/resource/domain/vavai/projekt/
n4http://linked.opendata.cz/resource/domain/vavai/riv/tvurce/
n19http://linked.opendata.cz/ontology/domain/vavai/
shttp://schema.org/
skoshttp://www.w3.org/2004/02/skos/core#
rdfshttp://www.w3.org/2000/01/rdf-schema#
n3http://linked.opendata.cz/ontology/domain/vavai/riv/
n17http://bibframe.org/vocab/
n2http://linked.opendata.cz/resource/domain/vavai/vysledek/
n8http://linked.opendata.cz/resource/domain/vavai/vysledek/RIV%2F00216224%3A14740%2F14%3A00073859%21RIV15-MSM-14740___/
rdfhttp://www.w3.org/1999/02/22-rdf-syntax-ns#
n5http://linked.opendata.cz/ontology/domain/vavai/riv/klicoveSlovo/
n16http://linked.opendata.cz/ontology/domain/vavai/riv/duvernostUdaju/
xsdhhttp://www.w3.org/2001/XMLSchema#
n14http://linked.opendata.cz/ontology/domain/vavai/riv/aktivita/
n11http://linked.opendata.cz/ontology/domain/vavai/riv/jazykVysledku/
n15http://linked.opendata.cz/ontology/domain/vavai/riv/druhVysledku/
n9http://linked.opendata.cz/ontology/domain/vavai/riv/obor/
n12http://reference.data.gov.uk/id/gregorian-year/

Statements

Subject Item
n2:RIV%2F00216224%3A14740%2F14%3A00073859%21RIV15-MSM-14740___
rdf:type
skos:Concept n19:Vysledek
rdfs:seeAlso
http://link.springer.com/article/10.1007%2Fs10822-014-9774-7
dcterms: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.
dcterms: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
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
skos:notation
RIV/00216224:14740/14:00073859!RIV15-MSM-14740___
n3:aktivita
n14:S n14:P
n3:aktivity
P(ED1.1.00/02.0068), P(GA13-25401S), P(LH13055), S
n3:cisloPeriodika
9
n3:dodaniDat
n12:2015
n3:domaciTvurceVysledku
n4:5522064 n4:4347374 n4:7678037 n4:6666477 n4:9309616 Chatzipavlou, Thomais Zotos, Petros
n3:druhVysledku
n15:J
n3:duvernostUdaju
n16:S
n3:entitaPredkladatele
n8:predkladatel
n3:idSjednocenehoVysledku
14640
n3:idVysledku
RIV/00216224:14740/14:00073859
n3:jazykVysledku
n11:eng
n3:klicovaSlova
Lectin; Carbohydrate; Mutagenesis; Docking; Molecular dynamics
n3:klicoveSlovo
n5:Mutagenesis n5:Lectin n5:Docking n5:Molecular%20dynamics n5:Carbohydrate
n3:kodStatuVydavatele
CH - Švýcarská konfederace
n3:kontrolniKodProRIV
[F2AAB0A820E1]
n3:nazevZdroje
Journal of Computer-Aided Molecular Design
n3:obor
n9:CE
n3:pocetDomacichTvurcuVysledku
7
n3:pocetTvurcuVysledku
7
n3:projekt
n13:ED1.1.00%2F02.0068 n13:LH13055 n13:GA13-25401S
n3:rokUplatneniVysledku
n12:2014
n3:svazekPeriodika
28
n3:tvurceVysledku
Mrázková, Jana Zotos, Petros Chatzipavlou, Thomais Kříž, Zdeněk Wimmerová, Michaela Adam, Jan Koča, Jaroslav
n3:wos
000342439000006
s:issn
0920-654X
s:numberOfPages
10
n17:doi
10.1007/s10822-014-9774-7
n20:organizacniJednotka
14740