V. V. Hurmach¹, M. O. Platonov², Yu. I. Prylutskyy¹

¹Taras Shevchenko National University of Kyiv, Ukraine;
²Institute of Molecular Biology and Genetics,
National Academy of Sciences of Ukraine, Kyiv;
e-mail: gyrmach@gmail.com

The conformational changes of proteins play an important role in biological functioning such as ligand-protein and protein-protein interactions. The aim of the work was to investigate the conformational movement of most represented SH2 domains. It was found that SH2 domain binding pocket includes both flexible and not flexible regions: the central area of the binding pocket is the most unflexible, whereas the pTyr-binding and hydrophobic zones are the most flexible. Results of the computer analysis revealed new conformational properties of SH2 domain, which are important for drug design.