Rearrangements in a hydrophobic core region mediate cAMP action in the regulatory subunit of PKA
{{output}}
cAMP-dependent protein kinase (PKA) forms an inactive heterotetramer of two regulatory (R; with two cAMP-binding domains A and B each) and two catalytic (C) subunits. Upon the binding of four cAMP molecules to the R dimer, the monomeric C subunits dissociate. ... ...
