Three protein kinase structures define a common motif.

Structural comparisons between cAMP-dependent protein kinase, cyclin-dependent kinase 2 and mitogen-activated protein kinase reveal which features are common to the protein kinase family and which are enzyme-specific.

[1]  D. Knighton,et al.  Structural basis of the intrasteric regulation of myosin light chain kinases. , 1992, Science.

[2]  E. Goldsmith,et al.  Crystallization and preliminary X-ray studies of extracellular signal-regulated kinase-2/MAP kinase with an incorporated His-tag. , 1993, Journal of molecular biology.

[3]  T. Hunter,et al.  The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. , 1988, Science.

[4]  K. Vrana,et al.  Adenosine cyclic 3',5'-monophosphate dependent protein kinase: kinetic mechanism for the bovine skeletal muscle catalytic subunit. , 1982, Biochemistry.

[5]  J. Zheng,et al.  Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. , 1991, Science.

[6]  A. Smith,et al.  An active twenty-amino-acid-residue peptide derived from the inhibitor protein of the cyclic AMP-dependent protein kinase. , 1985, The Biochemical journal.

[7]  S. Taylor,et al.  A conserved helix motif complements the protein kinase core. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[8]  Elizabeth J. Goldsmith,et al.  Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution , 1994, Nature.

[9]  R. Huber,et al.  Phosphotransferase and substrate binding mechanism of the cAMP‐dependent protein kinase catalytic subunit from porcine heart as deduced from the 2.0 A structure of the complex with Mn2+ adenylyl imidodiphosphate and inhibitor peptide PKI(5‐24). , 1993, The EMBO journal.

[10]  D. Knighton,et al.  2.0 A refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with a peptide inhibitor and detergent. , 1993, Acta crystallographica. Section D, Biological crystallography.

[11]  D. Knighton,et al.  A three-dimensional model of the Cdc2 protein kinase: localization of cyclin- and Suc1-binding regions and phosphorylation sites , 1993, Molecular and cellular biology.

[12]  Sung-Hou Kim,et al.  Crystal structure of cyclin-dependent kinase 2 , 1993, Nature.

[13]  E. Krebs,et al.  Microtubule-associated protein 2 kinases, ERK1 and ERK2, undergo autophosphorylation on both tyrosine and threonine residues: implications for their mechanism of activation. , 1991, Proceedings of the National Academy of Sciences of the United States of America.

[14]  P. Nurse,et al.  Animal cell cycles and their control. , 1992, Annual review of biochemistry.

[15]  P. Russell,et al.  The cdc25 M-phase inducer: An unconventional protein phosphatase , 1992, Cell.

[16]  K. Titani,et al.  Sequence of two phosphorylated sites in the catalytic subunit of bovine cardiac muscle adenosine 3':5'-monophosphate-dependent protein kinase. , 1979, The Journal of biological chemistry.

[17]  C. Marshall,et al.  A dominant-negative mutant of raf blocks mitogen-activated protein kinase activation by growth factors and oncogenic p21ras. , 1993, The Journal of biological chemistry.

[18]  G. Draetta,et al.  Mutations at sites involved in Suc1 binding inactivate Cdc2 , 1991, Molecular and cellular biology.

[19]  P. Dent,et al.  Inhibition of the EGF-activated MAP kinase signaling pathway by adenosine 3',5'-monophosphate. , 1993, Science.

[20]  C. Crews,et al.  The primary structure of MEK, a protein kinase that phosphorylates the ERK gene product. , 1992, Science.

[21]  Susan S. Taylor,et al.  cAMP‐dependent protein kinase: Crystallographic insights into substrate recognition and phosphotransfer , 1994, Protein science : a publication of the Protein Society.

[22]  J. Zheng,et al.  Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. , 1991, Science.

[23]  Susan S. Taylor,et al.  cAMP-dependent protein kinase: framework for a diverse family of regulatory enzymes. , 1990, Annual review of biochemistry.

[24]  N. Xuong,et al.  Structure of the mammalian catalytic subunit of cAMP-dependent protein kinase and an inhibitor peptide displays an open conformation. , 1993, Acta crystallographica. Section D, Biological crystallography.

[25]  P. R. Sibbald,et al.  The P-loop--a common motif in ATP- and GTP-binding proteins. , 1990, Trends in biochemical sciences.

[26]  J. Harper,et al.  CAK, the p34cdc2 activating kinase, contains a protein identical or closely related to p40MO15. , 1993, The EMBO journal.

[27]  C. Lange-Carter,et al.  A divergence in the MAP kinase regulatory network defined by MEK kinase and Raf , 1993, Science.

[28]  J. Zheng,et al.  Structural framework for the protein kinase family. , 1992, Annual review of cell biology.

[29]  S. Taylor,et al.  Energetic limits of phosphotransfer in the catalytic subunit of cAMP-dependent protein kinase as measured by viscosity experiments. , 1992, Biochemistry.

[30]  Nguyen-Huu Xuong,et al.  Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with magnesium-ATP and peptide inhibitor , 1993 .

[31]  S. Taylor,et al.  Identification of phosphorylation sites in the recombinant catalytic subunit of cAMP-dependent protein kinase. , 1993, The Journal of biological chemistry.

[32]  J. Trewhella,et al.  Solution structure of the cAMP-dependent protein kinase catalytic subunit and its contraction upon binding the protein kinase inhibitor peptide. , 1993, Biochemistry.

[33]  S. Cook,et al.  Inhibition by cAMP of Ras-dependent activation of Raf. , 1993, Science.

[34]  P. Dent,et al.  Dual phosphorylation and autophosphorylation in mitogen-activated protein (MAP) kinase activation. , 1993, The Biochemical journal.

[35]  L. Johnson,et al.  The allosteric transition of glycogen phosphorylase , 1989, Nature.

[36]  E. Krebs,et al.  Multiple components in an epidermal growth factor-stimulated protein kinase cascade. In vitro activation of a myelin basic protein/microtubule-associated protein 2 kinase. , 1991, The Journal of biological chemistry.

[37]  Susan S. Taylor,et al.  Crystal structures of the myristylated catalytic subunit of cAMP‐dependent protein kinase reveal open and closed conformations , 1993, Protein science : a publication of the Protein Society.

[38]  P. Russell,et al.  Human Wee1 kinase inhibits cell division by phosphorylating p34cdc2 exclusively on Tyr15. , 1993, The EMBO journal.

[39]  Susan S. Taylor,et al.  2.2 A refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MnATP and a peptide inhibitor. , 1993, Acta crystallographica. Section D, Biological crystallography.

[40]  H. Shuntoh,et al.  Autoactivation of catalytic (C alpha) subunit of cyclic AMP-dependent protein kinase by phosphorylation of threonine 197 , 1993, Molecular and cellular biology.

[41]  J. Tainer,et al.  Human CksHs2 atomic structure: a role for its hexameric assembly in cell cycle control. , 1993, Science.

[42]  Nancy Y. Ip,et al.  ERKs: A family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF , 1991, Cell.