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Article

Unidirectional allostery in the regulatory subunit RIα facilitates efficient deactivation of protein kinase A.

Proceedings of the National Academy of Sciences of the United States of America - 1 Nov 2016

Guo Cong, Zhou Huan-Xiang

Abstract excerpt

The holoenzyme complex of protein kinase A is in an inactive state; activation involves ordered cAMP binding to two tandem domains of the regulatory subunit and release of the catalytic subunit. Deactivation has been less studied, during which the two cAMPs unbind from the regulatory subunit to allow association of the catalytic subunit to reform the holoenzyme complex. Unbinding of the cAMPs appears ordered as...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cyclic AMP

Share to Cyclic AMP-Dependent Protein Kinase RIalpha Subunit

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Source

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Identifiers

PMID: 27791125
DOI: 10.1073/pnas.1610142113
PMCID: PMC5098638

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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