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:

You are running an old browser version. We recommend updating your browser to its latest version.