Engineering the Pseudomonas aeruginosa II lectin: designing mutants with changed affinity and specificity
| Authors | |
|---|---|
| Year of publication | 2014 |
| Type | Article in Periodical |
| Magazine / Source | Journal of Computer-Aided Molecular Design |
| MU Faculty or unit | |
| Citation | |
| web | http://link.springer.com/article/10.1007%2Fs10822-014-9774-7 |
| Doi | http://dx.doi.org/10.1007/s10822-014-9774-7 |
| Field | Biochemistry |
| Keywords | Lectin; Carbohydrate; Mutagenesis; Docking; Molecular dynamics |
| 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. |
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