Importance of oligomerisation on Pseudomonas aeruginosa Lectin-II binding affinity. In silico and in vitro mutagenesis.

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Authors	WIMMEROVÁ Michaela MISHRA Navnit Kumar POKORNÁ Martina KOČA Jaroslav
Year of publication	2009
Type	Article in Periodical
Magazine / Source	Journal of Molecular Modeling
MU Faculty or unit	Faculty of Science
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.
Related projects:	Proteins in metabolism and interaction of organisms with the environment Biomolecular centre Design of Carbohydrates and Glycomimetics as Antibacterial and Antiviral Drugs