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Protein kinases--structure and function Bossemeyer DFEBS Lett 1995[Aug]; 369 (1): 57-61The 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.|Amino Acid Sequence[MESH]|Binding Sites[MESH]|Casein Kinases[MESH]|Crystallography[MESH]|Cyclic AMP-Dependent Protein Kinases/chemistry/metabolism/physiology[MESH]|Models, Molecular[MESH]|Molecular Sequence Data[MESH]|Protein Kinases/chemistry/metabolism/*physiology[MESH]|Receptor, Insulin/chemistry/metabolism/physiology[MESH]|Structure-Activity Relationship[MESH] |
