Publication details
Importance of oligomerisation on Pseudomonas aeruginosa Lectin-II binding affinity. In silico and in vitro mutagenesis.
| Authors | |
|---|---|
| Year of publication | 2009 |
| Type | Article in Periodical |
| Magazine / Source | Journal of Molecular Modeling |
| MU Faculty or unit | |
| Citation | |
| Field | Biophysics |
| Keywords | protein-carbohydrate interaction; computational chemistry |
| Description | The effect of terminal GLY114* deletion on the binding affinity of the PA-IIL lectin towards L fucose was investigated. Both experimental (Isothermal Titration Calorimetry) and computational (Molecular dynamics simulations) methods have shown that the deletion mutation decreases the L fucose affinity. It implies that the PA-IIL saccharide binding affinity is influenced by the dimerization of the lectin. A detailed analysis of computational data confirms the key role of electrostatic interactions in the PA-IIL/saccharide binding. |
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