Using Markov state models to develop a mechanistic understanding of protein kinase A regulatory subunit RIα activation in response to cAMP binding.

@article{Boras2014UsingMS,
  title={Using Markov state models to develop a mechanistic understanding of protein kinase A regulatory subunit RIα activation in response to cAMP binding.},
  author={Britton W. Boras and Alexandr Kornev and Susan S. Taylor and Andrew D. McCulloch},
  journal={The Journal of biological chemistry},
  year={2014},
  volume={289 43},
  pages={30040-51}
}
Protein kinase A (PKA) holoenzyme consists of two catalytic (C) subunits and a regulatory (R) subunit dimer (R(2)C(2)). The kinase is activated by the binding of cAMPs to the two cyclic nucleotide binding domains (CBDs), A and B, on each R-subunit. Despite extensive study, details of the allosteric mechanisms underlying the cooperativity of holoenzyme activation remain unclear. Several Markov state models of PKA-RIα were developed to test competing theories of activation for the R(2)C(2… CONTINUE READING

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