Phosphorylation releases constraints to domain motion in ERK2.

@article{Xiao2014PhosphorylationRC,
  title={Phosphorylation releases constraints to domain motion in ERK2.},
  author={Yao Xiao and Thomas Lee and Michael P Latham and Lisa Rose Warner and Akiko Tanimoto and Arthur Pardi and Natalie G Ahn},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2014},
  volume={111 7},
  pages={
          2506-11
        }
}
Protein motions control enzyme catalysis through mechanisms that are incompletely understood. Here NMR (13)C relaxation dispersion experiments were used to monitor changes in side-chain motions that occur in response to activation by phosphorylation of the MAP kinase ERK2. NMR data for the methyl side chains on Ile, Leu, and Val residues showed changes in conformational exchange dynamics in the microsecond-to-millisecond time regime between the different activity states of ERK2. In inactive… CONTINUE READING

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