Protein kinases--structure and function.
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.
Bossemeyer
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Department of Pathochemistry, German Cancer Research Centre, Heidelberg.
D000595:Amino Acid Sequence; D001665:Binding Sites; D047388:Casein Kinases; D003461:Crystallography; D017868:Cyclic AMP-Dependent Protein Kinases / Q000737:chemistry / Q000378:metabolism / Q000502:physiology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011494:Protein Kinases / Q000737:chemistry / Q000378:metabolism / Q000502:physiology*; D011972:Receptor, Insulin / Q000737:chemistry / Q000378:metabolism / Q000502:physiology; D013329:Structure-Activity Relationship
D011494:Protein Kinases; D011972:Receptor, Insulin; D047388:Casein Kinases; D017868:Cyclic AMP-Dependent Protein Kinases