Folding and activity of cAMP-dependent protein kinase mutants

FEBS Letters

Volumn 579, Issue 19, 2005, Pages 4049-4054

  Langer, Thomas ^a   Sreeramulu, Sridhar ^a   Vogtherr, Martin ^a   Elshorst, Bettina ^a   Betz, Marco ^a   Schieborr, Ulrich ^a   Saxena, Krishna ^a   Schwalbe, Harald ^a  

^a GOETHE UNIVERSITY   (Germany)

Author keywords

Akt; Nuclear magnetic resonance; PKA; Protein kinase A; Protein phosphorylation

Indexed keywords

CYCLIC AMP; PROTEIN KINASE;

ARTICLE; BINDING SITE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE MUTATION; GENE SEQUENCE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PHOSPHORYLATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN FOLDING; SEQUENCE HOMOLOGY; WILD TYPE;

CYCLIC AMP-DEPENDENT PROTEIN KINASES; ESCHERICHIA COLI; MODELS, MOLECULAR; MUTATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEIN FOLDING; RECOMBINANT PROTEINS;

ESCHERICHIA COLI;

EID: 22544487801     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2005.06.015     Document Type: Article

References (15)

1. D. Fabbro, S. Ruetz, E. Buchdunger, S. Cowan-Jacob, G. Fendrich, J. Liebetanz, J. Mestan, T. O'Reilly, P. Traxler, B. Chaudhuri, H. Fretz, J. Zimmermann, T. Meyer, G. Caravatti, P. Furet, and P. Manley Protein kinases as targets for anticancer targets: from inhibitors to useful drugs Pharmacol. Therap. 93 2002 79 98
2. M.E.M. Noble, J.A. Endicott, and L.N. Johnson Protein kinase inhibitors: insight into drug design from structure Science 303 2004 1800 1805
3. R. Ren Mechanisms of BCR-ABL in the pathogenesis of chronic myelogenous leukaemia Nat. Rev. Cancer 5 2005 172 183
4. A. Birnbaum, and N. Ready Gefitinib therapy for non-small cell lung cancer Curr. Treat. Options Oncol. 6 2005 75 81
5. J. Brognard, A.S. Clark, Y. Ni, and P.A. Dennis Akt/protein kinase B is constitutively active in non-small cell lung cancer cells and promotes cellular survival and resistance to chemotherapy and radiation Cancer Res. 61 2001 3986 3997
6. M. Hanada, J. Feng, and B.A. Hemmings Structure, regulation and function of PKB/AKT - a major therapeutic target Biochim. Biophys. Acta 1697 2004 3 16
7. M. Gassel, C.B. Breitenlechner, P. Ruger, U. Jucknischke, T. Schneider, R. Huber, D. Bossemeyer, and R.A. Engh Mutants of protein kinase A that mimic the ATP-binding site of protein kinase B (AKT) J. Mol. Biol. 329 2003 1021 1034
8. C.B. Breitenlechner, W.G. Friebe, E. Brunet, G. Werner, K. Graul, U. Thomas, K.P. Kunkele, W. Schafer, M. Gassel, D. Bossemeyer, R. Huber, R.A. Engh, and B. Masjost Design and crystal structures of protein kinase B-selective inhibitors in complex with protein kinase A and mutants J. Med. Chem. 48 2005 163 170
9. C. Breitenlechner, M. Gassel, H. Hidaka, V. Kinzel, R. Huber, R.A. Engh, and D. Bossemeyer Protein kinase A in complex with Rho-kinase inhibitors Y-27632, Fasudil, and H-1152P: structural basis of selectivity Structure 11 2003 1595 1607
10. F.W. Herberg, S.M. Bell, and S.S. Taylor Expression of the catalytic subunit of cAMP-dependent protein kinase in Escherichia coli: multiple isozymes reflect different phosphorylation states Prot. Eng. 6 1993 771 777
11. W. Yonemoto, M.L. McGlone, B. Grant, and S.S. Taylor Autophosphorylation of the catalytic subunit of cAMP-dependent protein kinase in Escherichia coli Prot. Eng. 10 1997 915 925
12. 31P NMR spectroscopy Biochemistry 41 2002 5968 5977
13. T. Langer, M. Vogtherr, B. Elshorst, M. Betz, U. Schieborr, K. Saxena, and H. Schwalbe NMR backbone assignment of a protein kinase catalytic domain by a combination of several approaches: application to the catalytic subunit of cAMP-dependent protein kinase Chembiochem 5 2004 1508 1516
14. C.B. Breitenlechner, R.A. Engh, R. Huber, V. Kinzel, D. Bossemeyer, and M. Gassel The typically disordered N-terminus of PKA can fold as a helix and project the myristoylation site into solution Biochemistry 43 2004 7743 7749
15. K. Pervushin, R. Riek, G. Wider, and K. Wüthrich Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution Proc. Natl. Acad. Sci. USA 94 1997 12366 12371