Article
Switching of the folding-energy landscape governs the allosteric activation of protein kinase A.
Proceedings of the National Academy of Sciences of the United States of America - 7 Aug 2018
England Jeneffer P, Hao Yuxin, Bai Lihui, Glick Virginia, Hodges H Courtney, Taylor Susan S, Maillard Rodrigo A
Abstract excerpt
Protein kinases are dynamic molecular switches that sample multiple conformational states. The regulatory subunit of PKA harbors two cAMP-binding domains [cyclic nucleotide-binding (CNB) domains] that oscillate between inactive and active conformations dependent on cAMP binding. The cooperative binding of cAMP to the CNB domains activates an allosteric interaction network that enables PKA to progress from the...
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