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. Author manuscript; available in PMC: 2017 Mar 29.
Published in final edited form as: Biochemistry. 2016 Mar 16;55(12):1909–1917. doi: 10.1021/acs.biochem.6b00096

Figure 3.

Figure 3

Analysis of activities of ERK2 and T188 phosphomimetic substitutions. (A) MBP kinase assay with wild type ERK2 and kinase-dead ERK2 K52R compared to ERK2 T188D and T188E. (B) MEK1R4F phosphorylation of ERK2 and mutants. Recombinant Y185F is phosphorylated less well by MEK127. (C) Comparison of ERK2 or T188D kinase activities following activation by MEK1R4F with known ERK2 substrates. Phosphorylated substrates are denoted by wedges and phosphorylated ERK2 and T188 by asterisks. (D) Kinase activities of ERK2 T188D and T188E towards ERKtide. (E) Free energy profiles for ERK2 T188 migration from equilibrium position to a more ATP-Pγ-proximal position construed by molecular dynamics analysis.