[Simulation of kinase CDK2-cyclin A by the molecular dynamics method: effect of Gly16-->Ser16 and Arg274-->Gln274 substitutions on conformation of a kinase subunit].

The nanosecond-long molecular dynamics of the movement of the active protein kinase CDK2/ATP complex has been analyzed. The simulations of substitutions CDK2-G16S in the conserved G-loop of a small lobe and CDK2-R274Q in a large lobe showed the importance of the amino acid residues in the conformation of kinase and their effect on the conformation of CDK2, which shows up in an increase in the distance between G- and T-loops in the corresponding mutant forms. The results obtained indicate that the induction of both Gly16-->Ser16 and Arg274-->Gln274 mutations destabilize the local structure of kinase around the T-loop area. The mutation Arg274-->Gln274 has a more pronounced effect and results in a loosening of the structure of kinase and an increase of the distance between G- and T-loops.