PROTEIN-KINASES AND PHOSPHATASES - REGULATION BY AUTOINHIBITORY DOMAINS

Numerous enzymes which can be activated by allosteric ligands appear t o contain autoinhibitory domains which, through interaction with the c atalytic domains, maintain the enzymes in their inactive states. Bindi ng of activator ligands alters the conformation of the autoinhibitory domain and neutralizes its inhibitory potency, thereby producing enzym e activation. Such autoinhibitory domains have been -intensively studi ed in several protein kinases and phosphatases. This review summarizes our current understanding of these autoinhibitory domains in selected protein kinases and phosphatases.