Backbone resonance assignment of the cAMP-binding domains of the protein kinase A regulatory subunit Iα.

Biomolecular NMR Assignments
E Tyler McNichollGiuseppe Melacini

Abstract

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).

References

Nov 1, 1995·Journal of Biomolecular NMR·F DelaglioA Bax
Dec 26, 2001·Chemical Reviews·J B Shabb
Mar 26, 2003·Journal of Biomolecular NMR·Haiyan ZhangDavid S Wishart
May 27, 2003·Journal of Biomolecular NMR·Stephen NealDavid S Wishart
Dec 25, 2004·Proceedings of the National Academy of Sciences of the United States of America·Helen M BermanSusan S Taylor
Oct 4, 2006·Journal of Biomolecular NMR·Veronica EspositoGiuseppe Melacini
Nov 1, 2006·The Journal of Biological Chemistry·Rahul Das, Giuseppe Melacini
Dec 22, 2006·Proceedings of the National Academy of Sciences of the United States of America·Rahul DasGiuseppe Melacini
May 1, 2009·The Journal of Biological Chemistry·Rahul DasGiuseppe Melacini
Aug 16, 2013·Proceedings of the National Academy of Sciences of the United States of America·Madoka AkimotoGiuseppe Melacini
Sep 17, 2020·Science Advances·J A ByunG Melacini
May 20, 2021·Proceedings of the National Academy of Sciences of the United States of America·Naeimeh JafariGiuseppe Melacini

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