Backbone resonance assignment of the cAMP-binding domains of the protein kinase A regulatory subunit Iα Journal Articles uri icon

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  • Protein kinase A (PKA) is the main receptor for the universal cAMP second messenger. PKA is a tetramer with two catalytic (C) and two regulatory (R) subunits, each including two tandem cAMP-binding domains, i.e. CBD-A and -B. Activation of the complex occurs with cAMP binding first to CBD-B, followed by a second molecule of cAMP binding to CBD-A, which causes the release of the active C-subunit. Unlike previous constructs for eukaryotic cAMP-binding domains (CBDs), the 29.5 kDa construct analyzed here [i.e. RIα (119-379)] spans the CBDs in full and provides insight into inter-domain communication. In this note we report the 1H, 13C, and 15 N backbone assignments of cAMP-bound RIα (119-379) CBDs (BMRB No. 50920).


  • McNicholl, Eric Tyler
  • Das, Rahul
  • SilDas, Soumita
  • Byun, Jung Ah
  • Akimoto, Madoka
  • Jafari, Naeimeh
  • Melacini, Giuseppe

publication date

  • October 2021