Cyclic AMP analog blocks kinase activation by stabilizing inactive conformation: conformational selection highlights a new concept in allosteric inhibitor design.

@article{Badireddy2011CyclicAA,
  title={Cyclic AMP analog blocks kinase activation by stabilizing inactive conformation: conformational selection highlights a new concept in allosteric inhibitor design.},
  author={Suguna Badireddy and Gao Yunfeng and Mark Ritchie and Pearl Akamine and Jian Wu and Choel W Kim and Susan S. Taylor and Lin Qingsong and Kunchithapadam Swaminathan and Ganesh Srinivasan Anand},
  journal={Molecular & cellular proteomics : MCP},
  year={2011},
  volume={10 3},
  pages={M110.004390}
}
The regulatory (R) subunit of protein kinase A serves to modulate the activity of protein kinase A in a cAMP-dependent manner and exists in two distinct and structurally dissimilar, end point cAMP-bound "B" and C-subunit-bound "H"-conformations. Here we report mechanistic details of cAMP action as yet unknown through a unique approach combining x-ray crystallography with structural proteomics approaches, amide hydrogen/deuterium exchange and ion mobility mass spectrometry, applied to the study… CONTINUE READING

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