Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The conformationally dynamic C helix of the RIalpha subunit of protein kinase A mediates isoform-specific domain reorganization upon C subunit binding.

The Journal of biological chemistry - 21 Oct 2005

Vigil Dominico, Blumenthal Donald K, Taylor Susan S, Trewhella Jill

Abstract excerpt

Different isoforms of the full-length protein kinase A (PKA) regulatory subunit homodimer (R2) and the catalytic (C) subunit-bound holoenzyme (R2C2) have very different global structures despite similar molecular weights and domain organization within their primary sequences. To date, it has been the linker sequence between the R subunit dimerization/docking domain and cAMP-binding domain A that has been...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Catalysis
Share to Catalytic Domain

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cyclic AMP

Share to Cyclic AMP-Dependent Protein Kinase RIalpha Subunit

Share to Cyclic AMP-Dependent Protein Kinases

Share to Dimerization

Share to Scattering, Radiation

Share to X-Rays

Source

Identifiers

PMID: 16109722
DOI: 10.1074/jbc.M506769200

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The conformationally dynamic C helix of the RIalpha subunit of protein kinase A mediates isoform-specific domain reorganization upon C subunit binding.PMID 16109722Read ↗

The roles of the RIIβ linker and N-terminal cyclic nucleotide-binding domain in determining the unique structures of the type IIβ protein kinase A: a small angle x-ray and neutron scattering study.Semantic proximity Read ↗

PKA RIα homodimer structure reveals an intermolecular interface with implications for cooperative cAMP binding and Carney complex disease.Semantic proximity Read ↗

cAMP-dependent protein kinase regulatory subunit type IIbeta: active site mutations define an isoform-specific network for allosteric signaling by cAMP.Semantic proximity Read ↗

Realizing the allosteric potential of the tetrameric protein kinase A RIα holoenzyme.Semantic proximity Read ↗

Communication between tandem cAMP binding domains in the regulatory subunit of protein kinase A-Ialpha as revealed by domain-silencing mutations.Semantic proximity Read ↗

Dissecting interdomain communication within cAPK regulatory subunit type IIbeta using enhanced amide hydrogen/deuterium exchange mass spectrometry (DXMS).Semantic proximity Read ↗

Structure of D-AKAP2:PKA RI complex: insights into AKAP specificity and selectivity.Semantic proximity Read ↗

Interaction of the regulatory and catalytic subunits of cAMP-dependent protein kinase. Electrostatic sites on the type Ialpha regulatory subunit.Semantic proximity Read ↗

Consequences of cAMP and catalytic-subunit binding on the flexibility of the A-kinase regulatory subunit.Semantic proximity Read ↗

Mapping the Free Energy Landscape of PKA Inhibition and Activation: A Double-Conformational Selection Model for the Tandem cAMP-Binding Domains of PKA RIα.Semantic proximity Read ↗

Allosteric modulation of protein kinase A in individuals affected by NLPD-PKA, a neurodegenerative disease in which the RIβ-L50R variant is expressedSemantic proximity Read ↗

Unidirectional allostery in the regulatory subunit RIα facilitates efficient deactivation of protein kinase A.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.