. "9" . . "P(ED1.1.00/02.0068), P(GA13-25401S), P(LH13055), S" . "Mr\u00E1zkov\u00E1, Jana" . "0920-654X" . "000342439000006" . "14640" . . "Zotos, Petros" . "RIV/00216224:14740/14:00073859" . . "RIV/00216224:14740/14:00073859!RIV15-MSM-14740___" . "Engineering the Pseudomonas aeruginosa II lectin: designing mutants with changed affinity and specificity"@en . "Lectin; Carbohydrate; Mutagenesis; Docking; Molecular dynamics"@en . . "Chatzipavlou, Thomais" . "28" . . . "K\u0159\u00ED\u017E, Zden\u011Bk" . "Journal of Computer-Aided Molecular Design" . "[F2AAB0A820E1]" . "7"^^ . "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\u201323\u201324 (so-called specificity-binding loop), saturation in silico mutagenesis was performed, with the intent of finding mutations that increase the lectin\u2019s 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 . . . "Engineering the Pseudomonas aeruginosa II lectin: designing mutants with changed affinity and specificity" . . "7"^^ . . . "Engineering the Pseudomonas aeruginosa II lectin: designing mutants with changed affinity and specificity"@en . "Wimmerov\u00E1, Michaela" . . . "Adam, Jan" . "Ko\u010Da, Jaroslav" . . "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\u201323\u201324 (so-called specificity-binding loop), saturation in silico mutagenesis was performed, with the intent of finding mutations that increase the lectin\u2019s 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." . "10"^^ . . . . "CH - \u0160v\u00FDcarsk\u00E1 konfederace" . . "Chatzipavlou, Thomais" . "Engineering the Pseudomonas aeruginosa II lectin: designing mutants with changed affinity and specificity" . . . . "10.1007/s10822-014-9774-7" . "http://link.springer.com/article/10.1007%2Fs10822-014-9774-7" . . "Zotos, Petros" . . "14740" .