The structures of four serine/threonine protein kinases have been dete
rmined recently. By comparing these structures with that of the cAMP-d
ependent protein kinase (cAPK), it is now possible to see how the acti
vity of these regulatory enzymes is controlled. Low activity is mainta
ined through the conformation of the phosphorylation lip, domain rotat
ions, and binding of substrate analog inhibitors and autoinhibitory do
mains.