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Backbone resonance assignment of the cAMP-binding...
Journal article

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

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 …

Authors

McNicholl ET; Das R; SilDas S; Byun JA; Akimoto M; Jafari N; Melacini G

Journal

Biomolecular NMR Assignments, Vol. 15, No. 2, pp. 379–382

Publisher

Springer Nature

Publication Date

10 2021

DOI

10.1007/s12104-021-10033-8

ISSN

1874-2718