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Protein kinase C: Structural and spatial regulation by phosphorylation, cofactors, and macromolecular interactions

被引：810
作者：
Newton, AC [1 ]
机构：
[1] Univ Calif San Diego, Dept Pharmacol, La Jolla, CA 92093 USA
来源：
CHEMICAL REVIEWS | 2001年 / 101卷 / 08期
关键词：
D O I：
10.1021/cr0002801
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
The structural and spatial regulation of protein kinase C by phosphorylation cofactors and macromolecular interactions were studied. The phosphorylated species was maintained in an inactive conformation because the pseudosubstrate occupied the substrate-binding cavity. The results showed that the energy provided by the interaction of domains with the membrane released the pseudosubstrate which allowed substrate binding and phosphorylation.
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页码：2353 / 2364
页数：12
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