Crystal structures of the catalytic subunit of cAMP-dependent protein kinase reveal general features of the protein kinase family.
The crystal structure of the catalytic subunit of cAMP-dependent protein kinase serves as a template for the catalytic core of all eukaryotic protein kinases. The various crystal structures are reviewed with particular emphasis on the numerous conserved residues that converge at the active site. The structures also reveal the importance of posttranslational modifications, including myristylation and phosphorylation.
Taylor
S S
SS
Department of Chemistry, University of California, San Diego.
Radzio-Andzelm
E
E
Knighton
D R
DR
Ten Eyck
L F
LF
Sowadski
J M
JM
Herberg
F W
FW
Yonemoto
W
W
Zheng
J
J
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002384:Catalysis; D003460:Crystallization; D017868:Cyclic AMP-Dependent Protein Kinases / Q000737:chemistry*; D008969:Molecular Sequence Data; D011494:Protein Kinases / Q000737:chemistry*; D011499:Protein Processing, Post-Translational; D017386:Sequence Homology, Amino Acid
D011494:Protein Kinases; D017868:Cyclic AMP-Dependent Protein Kinases