title: Crystal structure of casein kinase-1, a phosphate-directed protein kinase.
abstract: The structure of a truncated variant of casein kinase-1 from Schizosaccharomyces pombe, has been determined in complex with MgATP at 2.0 A resolution. The model resembles the 'closed', ATP-bound conformations of the cyclin-dependent kinase 2 and the cAMP-dependent protein kinase, with clear differences in the structure of surface loops that impart unique features to casein kinase-1. The structure is of unphosphorylated, active conformation of casein kinase-1 and the peptide-binding site is fully accessible to substrate.
authors.affiliation: W.M. Keck Structural Biology Laboratory, Cold Spring Harbor, NY 11724.
authors.forename: R M
authors.initials: RM
authors.lastname: Xu
authors.forename: G
authors.initials: G
authors.lastname: Carmel
authors.forename: R M
authors.initials: RM
authors.lastname: Sweet
authors.forename: J
authors.initials: J
authors.lastname: Kuret
authors.forename: X
authors.initials: X
authors.lastname: Cheng
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D001665:Binding Sites; D047388:Casein Kinases; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010766:Phosphorylation; D011487:Protein Conformation; D011494:Protein Kinases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D012568:Schizosaccharomyces / Q000201:enzymology; D016415:Sequence Alignment; D017384:Sequence Deletion; D013379:Substrate Specificity
chemical_list: D000255:Adenosine Triphosphate; D011494:Protein Kinases; D047388:Casein Kinases