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Biochemistry. 2017 Aug 1;56(30):3885-3888. doi: 10.1021/acs.biochem.7b00461. Epub 2017 Jul 17.

Molecular Simulations Reveal an Unresolved Conformation of the Type IA Protein Kinase A Regulatory Subunit and Suggest Its Role in the cAMP Regulatory Mechanism.

Author information

1
Department of Chemistry and Biochemistry and National Biomedical Computational Resource, University of California, San Diego , 9500 Gilman Drive, La Jolla, California 92093-0304, United States.

Abstract

We identify a previously unresolved, unrecognized, and highly stable conformation of the protein kinase A (PKA) regulatory subunit RIα. This conformation, which we term the "Flipback" structure, bridges conflicting characteristics in crystallographic structures and solution experiments of the PKA RIα heterotetramer. Our simulations reveal a hinge residue, G235, in the B/C helix that is conserved through all isoforms of RI. Brownian dynamics simulations suggest that the Flipback conformation plays a role in cAMP association to the A domain of the R subunit.

PMID:
28661131
PMCID:
PMC5751417
DOI:
10.1021/acs.biochem.7b00461
[Indexed for MEDLINE]
Free PMC Article

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