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@article{1198038,
author = {Kříž, Zdeněk and Adam, Jan and Mrázková, Jana and Zotos, Petros and Chatzipavlou, Thomais and Wimmerová, Michaela and Koča, Jaroslav},
article_location = {Dordrecht (Netherlands)},
article_number = {9},
doi = {http://dx.doi.org/10.1007/s10822-014-9774-7},
keywords = {Lectin; Carbohydrate; Mutagenesis; Docking; Molecular dynamics},
language = {eng},
issn = {0920-654X},
journal = {Journal of Computer-Aided Molecular Design},
title = {Engineering the Pseudomonas aeruginosa II lectin: designing mutants with changed affinity and specificity},
url = {http://link.springer.com/article/10.1007%2Fs10822-014-9774-7},
volume = {28},
year = {2014}
}
TY - JOUR
ID - 1198038
AU - Kříž, Zdeněk - Adam, Jan - Mrázková, Jana - Zotos, Petros - Chatzipavlou, Thomais - Wimmerová, Michaela - Koča, Jaroslav
PY - 2014
TI - Engineering the Pseudomonas aeruginosa II lectin: designing mutants with changed affinity and specificity
JF - Journal of Computer-Aided Molecular Design
VL - 28
IS - 9
SP - 951-960
EP - 951-960
PB - Springer International Publishing
SN - 0920654X
KW - Lectin
KW - Carbohydrate
KW - Mutagenesis
KW - Docking
KW - Molecular dynamics
UR - http://link.springer.com/article/10.1007%2Fs10822-014-9774-7
L2 - http://link.springer.com/article/10.1007%2Fs10822-014-9774-7
N2 - 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.
ER -
KŘÍŽ, Zdeněk, Jan ADAM, Jana MRÁZKOVÁ, Petros ZOTOS, Thomais CHATZIPAVLOU, Michaela WIMMEROVÁ a Jaroslav KOČA. Engineering the Pseudomonas aeruginosa II lectin: designing mutants with changed affinity and specificity. \textit{Journal of Computer-Aided Molecular Design}. Dordrecht (Netherlands): Springer International Publishing, roč.~28, č.~9, s.~951-960. ISSN~0920-654X. doi:10.1007/s10822-014-9774-7. 2014.
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