PROTEIN-KINASES - STRUCTURE AND FUNCTION

被引:94
作者
BOSSEMEYER, D
机构
关键词
CRYSTAL STRUCTURE; CAMP-DEPENDENT PROTEIN KINASE; PROTEIN KINASE CK1; INSULIN RECEPTOR; CATALYTIC SITE; CONSERVED SEQUENCE MOTIF;
D O I
10.1016/0014-5793(95)00580-3
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:57 / 61
页数:5
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