Figure 2.

Structure of PKA-RIα dimerization and docking domain (D/D-domain) in complex with D-AKAP2 [52] (PDB 3IM4). The RIα D/D-domain (blue and dark blue) is defined by an N-terminal helical bundle that promotes regulatory subunit dimerization via hydrophobic interactions. Under oxidative conditions, additional intermolecular disulfide bonds are formed by cysteines at position 17 and 38. The interaction with different AKAPs (grey) is mostly caused by hydrophobic interactions alongside salt bridges. An effect of the interdisulfide bond formation on D/D-domain-AKAP interaction and PKA localization could be shown by different studies [43,48].