A template for the protein kinase family.
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.
Taylor
S S
SS
Department of Chemistry, University of California, San Diego, La Jolla 92093-0654.
Knighton
D R
DR
Zheng
J
J
Sowadski
J M
JM
Gibbs
C S
CS
Zoller
M J
MJ
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
D011494:Protein Kinases