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Article

Interaction of the regulatory subunit (RII) of cAMP-dependent protein kinase with RII-anchoring proteins occurs through an amphipathic helix binding motif.

The Journal of biological chemistry - 5 Aug 1991

Carr D W, Stofko-Hahn R E, Fraser I D, Bishop S M, Acott T S, Brennan R G, Scott J D

Abstract excerpt

The type II cAMP-dependent protein kinase is localized to specific subcellular environments through the binding of the regulatory subunit (RII) dimer to RII-anchoring proteins. Computer-aided analysis of secondary structure, performed on four RII-anchoring protein sequences (the microtubule-associated protein 2, P150, and two thyroid proteins Ht 21 and Ht 31), has identified common regions of approximately 14...

Topics

A Kinase Anchor Proteins
Adaptor Proteins, Signal Transducing
Amino Acid Sequence
Carrier Proteins
Electrophoresis, Polyacrylamide Gel
Escherichia coli
Humans
Molecular Sequence Data
Mutagenesis, Site-Directed

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Protein Binding

Protein Kinases

Recombinant Proteins

Sequence Homology, Nucleic Acid

Source

Identifiers

PMID: 1860836

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1860836-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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