Protein kinases — structure and function

• Published in: FEBS Letters Vol. 369; no. 1; pp. 57 - 61
• Main Author: Bossemeyer, Dirk
• Format: Book Review Journal Article
• Language: English
• Published: England Elsevier B.V 01-08-1995
• Subjects: Amino Acid Sequence; Binding Sites; cAMP-dependent protein kinase; cAPK; Casein Kinases; Catalytic site; CDK2; CK1; CKil; Conserved sequence motif; Crystal structure; Crystallography; Cyclic AMP-Dependent Protein Kinases - chemistry; Cyclic AMP-Dependent Protein Kinases - metabolism; Cyclic AMP-Dependent Protein Kinases - physiology; cyclin dependent kinase 2; ERK; extracellular signal regulated kinase; Insulin receptor; IRK; kinase domain fragment of insuline receptor; Models, Molecular; Molecular Sequence Data; Protein kinase CK1; protein kinase CK1, formerly casein kinase I; Protein Kinases - chemistry; Protein Kinases - metabolism; Protein Kinases - physiology; Receptor, Insulin - chemistry; Receptor, Insulin - metabolism; Receptor, Insulin - physiology; Residue numbers of homologous residues of cAPK are in brackets; Structure-Activity Relationship; variant of CK1; IRK; Protein kinase CK1; CK1; cAMP-dependent protein kinase; Conserved sequence motif; cAPK; CKil; CDK2; Catalytic site; Insulin receptor; Residue numbers of homologous residues of cAPK are in brackets; Crystal structure; ERK
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(95)00580-3

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.