Figure 2

Amino Acid Alignments of AKAP7 RI/RII binding domain and PKA-R D/D domains. Protein regions from the AKAP7 RI/RII binding domain (A), PKA-RIIα dimerization/Docking domain (D/D; B), PKA-RIα D/D (C) PKA-RIβ D/D, (D), and PKA-RIIβ (E) were aligned using Clustal X. (A) Residues in the AKAP7 RI/RII binding domain that have been previously identified as components of an amphipathic α-helix necessary for PKA-R subunit interaction are indicated by (*) and residues that are conserved are shaded. In the AKAP7 RI/RII binding domain, α-helix forming residues are conserved in vertebrates from lamprey to humans. Residues in the PKA-RIIα (B), PKA-RIα (C), PKA-RIβ (D), and PKA-RIIβ (E) D/D domains forming the docking surface for the AKAP helix which are highly conserved are indicated by shading. Residues in PKA-RIIα that are essential for AKAP binding [48, 49] are indicated by (*). The spacer region between helices in PKA-RIIα is indicated by a dotted line.