Taylor S S, Knighton D R, Zheng J, Ten Eyck L F, Sowadski J M
Department of Chemistry, University of California, San Diego, La Jolla 92093-0654.
Annu Rev Cell Biol. 1992;8:429-62. doi: 10.1146/annurev.cb.08.110192.002241.
In this review, we have summarized the general structural features of the catalytic subunit of cAMP-dependent protein kinase, emphasizing those features that will very likely be conserved in all members of the protein kinase family. The overall secondary structure of the catalytic core will probably be conserved throughout the catalytic core, as will the active site regions associated with MgATP binding and catalysis. The mechanisms for activation and the role of protein phosphorylation are unique for each kinase. The structure of the catalytic subunit now provides a general framework for modeling other protein kinases. Although this is no substitute for a crystal structure for each protein kinase, this one structure, nevertheless, does provide major insights to the molecular organization of each of these enzymes.
在本综述中，我们总结了环磷酸腺苷依赖性蛋白激酶催化亚基的一般结构特征，重点强调了那些很可能在蛋白激酶家族所有成员中保守的特征。催化核心的整体二级结构可能在整个催化核心中都是保守的，与MgATP结合及催化相关的活性位点区域也是如此。每种激酶的激活机制和蛋白质磷酸化的作用都是独特的。催化亚基的结构现在为其他蛋白激酶的建模提供了一个总体框架。虽然这不能替代每种蛋白激酶的晶体结构，但这一结构确实为深入了解这些酶中每一种的分子组织提供了重要线索。
