Molecular dynamics simulations of human kinase protein: the influence of a conserved glycine by serine substitution in the G-loop of a CDK2 active complex

We have performed the mutation analysis of functionally important structural elements for a cyclin dependent kinase protein via 2 ns molecular dynamics (MD) simulations of a crystal lattice of kinase active complex pT160-CDK2/cyclin A/ATP-Mg²⁺/substrate. Based on the MD simulation results we discuss the influence of the structural conformation changes on the kinase activity and molecular mechanism of regulation of phosphorylation.