FEBS Letters | |
Protein kinases — structure and function | |
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
【 预 览 】
Files | Size | Format | View |
---|---|---|---|
RO201912020301417ZK.pdf | 461KB | download |