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Background: The eukaryotic translation Elongation Factor 2 (eEF2) is a 95 kDa member of the G-protein superfamily. Following peptide bond formation, eEF2 catalyzes translocation of the deacylated tRNA in the P-site and peptidyl tRNA in the A-site into the E- and P- sites, respectively (1). The activity of eEF2 is regulated by phosphorylation (2). To be active, eEF2 must be dephosphorylated, and phosphorylation at Thr-56 causes inactivation, resulting in the termination of mRNA translation (3). eEF2 is phosphorylated by a specific, calcium and calmodulin (Ca/CaM)-dependent eEF2 kinase (4).