title: A template for the protein kinase family.
abstract: The crystal structure of the catalytic subunit of cAMP-dependent protein kinase, complexed with ATP and a 20-residue inhibitor peptide, is reviewed and correlated with chemical and genetic data. The striking convergence of the structure with the biochemistry and genetics provides for the first time a molecular basis for understanding how this enzyme functions, as well as an explanation for the highly conserved residues that are scattered throughout the molecule. Because these residues probably serve a common role in all eukaryotic protein kinases, this first protein kinase structure serves as a general template for the entire family of enzymes.
authors: Department of Chemistry, University of California, San Diego, La Jolla 92093-0654.
authors: S S
authors: SS
authors: Taylor
authors: D R
authors: DR
authors: Knighton
authors: J
authors: J
authors: Zheng
authors: J M
authors: JM
authors: Sowadski
authors: C S
authors: CS
authors: Gibbs
authors: M J
authors: MJ
authors: Zoller
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D008969:Molecular Sequence Data; D009154:Mutation; D011494:Protein Kinases / Q000737:chemistry* / Q000235:genetics; D017433:Protein Structure, Secondary; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics; D013329:Structure-Activity Relationship
chemical_list: D011494:Protein Kinases