Protein kinases — structure and function

FEBS Letters

Bossemeyer, Dirk¹ 

[1] Department of Pathochemistry, German Cancer Research Centre, INF 280, D-69120 Heidelberg, Germany

关键词: Crystal structure;    cAMP-dependent protein kinase;    Protein kinase CK1;    Insulin receptor;    Catalytic site;    Conserved sequence motif;    cAPK;    cAMP-dependent protein kinase;    CK1;    protein kinase CK1;    formerly casein kinase I;    CKil;    variant of CK1;    ERK;    extracellular signal regulated kinase;    IRK;    kinase domain fragment of insuline receptor;    CDK2;    cyclin dependent kinase 2;    Residue numbers of homologous residues of cAPK are in brackets;   

DOI  :  10.1016/0014-5793(95)00580-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown