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

@article{Carr1991InteractionOT,
  title={Interaction of the regulatory subunit (RII) of cAMP-dependent protein kinase with RII-anchoring proteins occurs through an amphipathic helix binding motif.},
  author={Daniel J J Carr and Renata E. Stofko-Hahn and Iain D Fraser and Stefan Mark Bishop and Ted S. Acott and Richard G Brennan and John D Scott},
  journal={The Journal of biological chemistry},
  year={1991},
  volume={266 22},
  pages={14188-92}
}
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 residues which display high probabilities of forming amphipathic helices. The… CONTINUE READING
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Protein Engineering (Oxender

S. Erickson-Viitanen, D. T. O’Neil, W. F. DeGrado
1987

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