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. Author manuscript; available in PMC: 2019 Mar 15.
Published in final edited form as: Bioorg Med Chem. 2018 Feb 12;26(6):1174–1178. doi: 10.1016/j.bmc.2018.02.001

Figure 1.

Figure 1

Targeted disruption of AKAP signaling complexes with constrained peptides. a) AKAP signaling complexes can scaffold a variety of different proteins in addition to PKA including adenylyl cyclases (ACs), phosphodiesterases (PDEs), substrates and protein phosphatases (PPases). The tetrameric holoenzyme complex interacts with an AKAP-derived helix through its regulatory domains. b) A hydrocarbon stapled peptide, STAD-2, was previously shown to selectively inhibit RII:AKAP complexes and was used as a template for library design. c) The constrained peptide is designed to inhibit the binding groove formed in the docking/dimerization (D/D) domain of the R-subunit of PKA (gray) that serves as a docking site for AKAPs (teal). In the STAD-2 sequence above, amino acids facing the D/D domain are depicted in red and solvent exposed amino acids are shown in teal.