NMR studies of the RRsrc peptide, a tyrosine kinase substrate

Biochemistry and Cell Biology

Volumn 75, Issue 2, 1997, Pages 163-169

  Brockbank, Ronald L ^a   Vogel, Hans J ^a  

^a UNIVERSITY OF CALGARY   (Canada)

Author keywords

Autophosphorylation; NMR; pp60src; Src; Tyrosine phosphorylation

Indexed keywords

PROTEIN KINASE P60;

ARTICLE; AUDIOVISUAL EQUIPMENT; CHEMISTRY; COMPARATIVE STUDY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; ONCOGENE SRC; PHOSPHORYLATION;

GENES, SRC; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, STRUCTURAL; PHOSPHORYLATION; PROTO-ONCOGENE PROTEINS PP60(C-SRC);

EID: 0030623611     PISSN: 08298211     EISSN: None     Source Type: Journal    
DOI: 10.1139/o97-028     Document Type: Article

References (21)

1. c-src. Biochem. Cell Biol. 74: 477-484.
2. Brockbank, R.L. 1993. NMR studies of phosphorylated peptides. Ph.D. thesis, University of Calgary, Calgary, Alta.
3. Brown, M.T., and Cooper, J.A. 1996. Regulation, substrates and functions of src. Biochim. Biophys. Acta, 1287: 121-149.
4. Casnellie, J.E., Harrison, M.L., Pike, L.J., Hellstrom, K.E., and Krebs, E.G. 1982. Phosphorylation of synthetic peptides by a tyrosine protein kinase from the particulate fraction of a lymphoma cell line. Proc. Natl. Acad. Sci. U.S.A. 79: 282-286.
5. Chakrabartty, A., and Baldwin, R.L. 1995. Stability of α-helices. Adv. Protein Chem. 46: 141-176.
6. Chakrabartty, A., Schellman, J.A., and Baldwin, R.L. 1991. Large differences in the helix propensities of alanine and glycine. Nature (London), 351: 586-588.
7. cdc2 is a specific and efficient substrate of src-family tyrosine kinases. J. Biol. Chem. 267: 9248-9256.
8. Chou, P. Y., and Fasman, G.D. 1978. Empirical predictions of protein conformations. Annu. Rev. Biochem. 47: 251-276.
9. Cooper, J.A., and Howell, B. 1993. The when and how of Src regulation. Cell, 73: 1051-1054.
10. c-src by intermolecular autophosphorylation. Proc. Natl. Acad. Sci. U.S.A. 85: 4232-4236.
11. Cooper, J.A., Esch, F.S., Taylor, S.S., and Hunter, T. 1984. Phosphorylation sites in enolase and lactate dehydrogenase utilized by tyrosine protein kinases in vivo and in vitro. J. Biol. Chem. 259: 7835-7841.
12. Courtneidge, S.A. 1994. Non-receptor protein-tyrosine kinases. In Protein kinases. Edited by J.R. Woodgett. IRL Press, Oxford. pp. 212-242.
13. Eck, M.J., Atwell, S.K., Shoelson, S.E., and Harrison, G.C. 1994. Structure of the regulatory domains of the src-family tyrosine kinase Lck. Nature (London), 368: 764-769.
14. Gaehlen, R.L., and Harrison, M.L. 1990. Protein tyrosine kinases. In Peptides and protein phosphorylation. CRC Press, Boca Raton, Fla. pp. 239-253.
15. Hubbard, S.R., Wei, L., Ellis, L., and Hendrickson, W.A. 1994. Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature (London), 372: 746-754.
16. Hunter, T., and Lindberg, R.A. 1994. Receptor protein-tyrosine kinases. In Protein kinases. Edited by J.R. Woodgett. IRL Press, Oxford, pp. 177-211.
17. src proteins expressed in yeast. Proc. Natl. Acad. Sci. U.S.A. 84: 4455-1459.
18. Levine, B.A., Clack, B., and Ellis, L. 1991. A soluble insulin receptor kinase catalyzes ordered phosphorylation at multiple tyrosines of dodeca-peptide substrates. J. Biol. Chem. 266: 3565-3570.
19. Mohammadi, M., Schlessinger, J., and Hubbard, S.R. 1996. Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism. Cell, 86: 577-587.
20. Molday, R.S., Englander, S.W., and Kallenbach, R.G. 1972. Primary structure effects on peptide group hydrogen exchange. Biochemistry, 11: 150-158.
21. O'Neill, K.T., and DeGrado, W.F. 1990. A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids. Science (Washington, D.C.), 250: 646-651.