Intrapeptide regulation of protein kinase C.
作者： AC NEWTON , LM KERANEN , JW ORR
DOI: 10.1016/S0021-9258(17)37205-8
关键词:
摘要: Protein kinase C is allosterically activated by diacylglycerol and phosphatidylserine. The enzyme also surprisingly dissimilar compounds such as short chained phosphatidylcholines protamine sulfate. Here we show that conventional nonconventional activators of protein beta II produce the same structural alteration. They expose Arg19 autoinhibitory pseudosubstrate domain to proteolysis. Molecular modeling II's catalytic domain, based on structure cAMP-dependent kinase's indicates shielded a cluster acidic residues when occupies substrate-binding site. Our biochemical data indicate common mechanism intrapeptide regulation all involves release from active
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