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

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F14%3A00073859" target="_blank" >RIV/00216224:14740/14:00073859 - isvavai.cz</a>

Výsledek na webu

<a href="http://link.springer.com/article/10.1007%2Fs10822-014-9774-7" target="_blank" >http://link.springer.com/article/10.1007%2Fs10822-014-9774-7</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s10822-014-9774-7" target="_blank" >10.1007/s10822-014-9774-7</a>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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 wasused. 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 23did not have strong effects thanks to the side chain being pointed away from the binding site.

Název v anglickém jazyce

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

Popis výsledku anglicky

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 wasused. 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 23did not have strong effects thanks to the side chain being pointed away from the binding site.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2014

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Computer-Aided Molecular Design

ISSN

0920-654X

e-ISSN

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Svazek periodika

28

Číslo periodika v rámci svazku

9

Stát vydavatele periodika

CH - Švýcarská konfederace

Počet stran výsledku

10

Strana od-do

951-960

Kód UT WoS článku

000342439000006

EID výsledku v databázi Scopus

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