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Article

Realizing the allosteric potential of the tetrameric protein kinase A RIα holoenzyme.

Structure (London, England : 1993) - 9 Feb 2011

Boettcher Angela J, Wu Jian, Kim Choel, Yang Jie, Bruystens Jessica, Cheung Nikki, Pennypacker Juniper K, Blumenthal Donald A, Kornev Alexandr P, Taylor Susan S

Abstract excerpt

PKA holoenzymes containing two catalytic (C) subunits and a regulatory (R) subunit dimer are activated cooperatively by cAMP. While cooperativity involves the two tandem cAMP binding domains in each R-subunit, additional cooperativity is associated with the tetramer. Of critical importance is the flexible linker in R that contains an inhibitor site (IS). While the IS becomes ordered in the R:C heterodimer, the...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 21300294
DOI: 10.1016/j.str.2010.12.005
PMCID: PMC3097484

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Realizing the allosteric potential of the tetrameric protein kinase A RIα holoenzyme.PMID 21300294Read ↗

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