title: Protein kinases.
abstract: The structures of four serine/threonine protein kinases have been determined recently. By comparing these structures with that of the cAMP-dependent protein kinase (cAPK), it is now possible to see how the activity of these regulatory enzymes is controlled. Low activity is maintained through the conformation of the phosphorylation lip, domain rotations, and binding of substrate analog inhibitors and autoinhibitory domains.
authors.affiliation: Department of Biochemistry, University of Texas Southwestern Medical Center at Dallas 75235.
authors.forename: E J
authors.initials: EJ
authors.lastname: Goldsmith
authors.forename: M H
authors.initials: MH
authors.lastname: Cobb
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011494:Protein Kinases / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D011494:Protein Kinases