PROTEIN-KINASES - STRUCTURE AND FUNCTION
PROTEIN-KINASES - STRUCTURE AND FUNCTION
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DOI：
10.1016/0014-5793(95)00580-3
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发表时间：
1995-08-01
期刊：
影响因子：
3.5
通讯作者：
BOSSEMEYER, D
中科院分区：
文献类型：
--
作者：
BOSSEMEYER, D
过去四年来在不同实验室的六种蛋白激酶的晶体结构的解决加深了我们对这类酶的催化和调节的理解，并有力地推动了整个领域的发展。由于蛋白激酶之间序列的高度保守性，每个新结构的信息量都很高，因为每个新结构都是酶家族的代表，而且通常是一个亚类。本文将重点介绍cAMP依赖的蛋白激酶(CAPK)的活性部位结构，特别是两个新的晶体结构：一个是活性蛋白激酶CK1*，它可能是动力学途径中尚未解决的一步；另一个是胰岛素受体激酶结构域，它是酪氨酸激酶的第一个结构。
The solution of crystal structures from half a dozen protein kinases during the last four years in different laboratories has deepened our understanding of the catalysis and regulation of this enzyme class, and given a vigorous impetus to the whole field. Due to the great degree of sequence conservation among protein kinases the informational yield with every new structure is high, as each is a representative of the enzyme family in general and most often of a subclass in particular, This review will focus on the active site structure of cAMP-dependent protein kinase (cAPK) with special regard to two new crystal structures; one of an active protein kinase CK1*, which may represent an as yet unsolved step in the kinetic pathway, and the other of the insulin receptor kinase domain, the first structure of a tyrosine kinase.