Báo cáo Y học: Electrostatic properties of the structure of the docking and dimerization domain of protein kinase A IIa

The structure of the N-terminal docking and dimerization domain of the type IIa regulatory subunit (RIIa D/D) of protein kinase A (PKA) forms a noncovalent stand-alone X-type four-helix bundle structural motif, consisting of two helix-loop-helix monomers. RIIa D/D possesses a strong hydrophobic core and two distinct, exposed faces. A hydrophobic face with a groove is the site of protein–protein interactions necessary for subcellular localization.