Ligand-induced global transitions in the catalytic domain of protein kinase A.

@article{Hyeon2009LigandinducedGT,
  title={Ligand-induced global transitions in the catalytic domain of protein kinase A.},
  author={Changbong Hyeon and Patricia Ann Jennings and Joseph A. Adams and Jos{\'e} N. Onuchic},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2009},
  volume={106 9},
  pages={3023-8}
}
Conformational transitions play a central role in the phosphorylation mechanisms of protein kinase. To understand the nature of these transitions, we investigated the dynamics of nucleotide binding to the catalytic domain of PKA, a prototype for the protein kinase enzyme family. The open-to-closed transition in PKA was constructed as a function of ATP association by using available X-ray data and Brownian dynamics. Analyzing the multiple kinetic trajectories at the residue level, we find that… CONTINUE READING

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