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. Author manuscript; available in PMC: 2016 Nov 1.
Published in final edited form as: Trends Biochem Sci. 2015 Oct 21;40(11):628–647. doi: 10.1016/j.tibs.2015.09.002

Figure 5.

Figure 5

Changes in slow dynamics in PKA and ERK2. (A) Nuclear spin relaxation rate (Rex), that reflects amino acid dynamics in µs-ms timescale, is mapped onto the PKA structure. Relatively low signal is detected in PKA with no nucleotide bound. (B) Binding of the ATP-analog AMP-PNP causes a significant increase of Rex throughout the whole molecule. (C) Binding of peptide inhibitor (PKI) leads to significant decrease of the slow dynamics. (Adapted from [26]) (D) Relaxation dispersion analysis of [13C]-labeled methyl groups provides information on dynamics in the µs-ms range in ERK2. Not phosphorylated form of ERK2 reveals diverse dynamic properties of hydrophobic sidechains in the range of 1–2kHz. (E) Double phosphorylation of the Activation Loop causes a significant decrease in the dynamics rate and leads to a more uniform dynamic profile of the kinase core. (Adapted from [84])