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

Warning

This publication doesn't include Faculty of Education. It includes Faculty of Science. Official publication website can be found on muni.cz.

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