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New conformational properties of SH2 domain binding pocket
2015
Ukrainian Biochemical Journal
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
doi:10.15407/ubj87.05.133
fatcat:4rlfnyzearfpra34fyst3htkrq