KŘÍŽ, Zdeněk, Jan ADAM, Jana MRÁZKOVÁ, Petros ZOTOS, Thomais CHATZIPAVLOU, Michaela WIMMEROVÁ and Jaroslav KOČA. Engineering the Pseudomonas aeruginosa II lectin: designing mutants with changed affinity and specificity. Journal of Computer-Aided Molecular Design. Dordrecht (Netherlands): Springer International Publishing, 2014, vol. 28, No 9, p. 951-960. ISSN 0920-654X. Available from: https://dx.doi.org/10.1007/s10822-014-9774-7. |
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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 and 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, 2014, vol.~28, No~9, p.~951-960. ISSN~0920-654X. Available from: https://dx.doi.org/10.1007/s10822-014-9774-7.
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