Crystal structures of c-Src reveal features of its autoinhibitory mechanism

Molecular Cell

Volumn 3, Issue 5, 1999, Pages 629-638

  Xu, Wenqing ^a   Doshi, Amish ^b   Lei, Ming ^c   Eck, Michael J ^d   Harrison, Stephen C ^e  

^a BOSTON CHILDREN S HOSPITAL   (United States)

^b HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^c HARVARD MEDICAL SCHOOL   (United States)

^d DANA FARBER CANCER INSTITUTE   (United States)

^e UNIVERSITY OF WASHINGTON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN TYROSINE KINASE; TYROSINE;

ALPHA HELIX; ARTICLE; AUTOREGULATION; BINDING SITE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME CONFORMATION; ENZYME INHIBITION; ENZYME SUBSTRATE; HUMAN; PROTEIN PHOSPHORYLATION;

EID: 0033001789     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(00)80356-1     Document Type: Article

References (39)

1. Alexandropoulos, K., and Baltimore, D. (1996). Coordinate activation of c-Src by SH3- and SH2- binding sites on a novel p130CAS-related protein, Sin. Genes Dev. 10, 1341-1355.
2. Boerner, R.J., Kassel, D.B., Barker, S.C., Ellis, B., DeLacy, P., and Knight, W.B. (1996). Correlation of the phosphorylation states of pp60 c-src with tyrosine kinase activity: the intramolecular pY530-SH2 complex retains significant activity if Y419 is phosphorylated. Biochemistry 35, 9519-9525.
3. Brown, M.T., and Cooper, J.A. (1996). Regulation, substrates and functions of src. Biochim. Biophys. Acta 1287, 121-149.
4. Brünger, A. (1992). X-PLOR Version 3.0: a System for Crystallography and NMR (New Haven, CT: Yale University Press).
5. Canagarajah, B.J., Khokhlatchev, A., Cobb, M.H., and Goldsmith, E.J. (1997). Activation mechanism of the MAP kinase ERK2 by dual phosphorylation. Cell 90, 859-869.
6. De Bondt, H.L., Rosenblatt, J., Jancarik, J., Jones, H.D., Morgan, D.O., and Kim, S.H. (1993). Crystal structure of cyclin-dependent kinase 2. Nature 363, 595-602.
7. Erpel, T., and Courtneidge, S.A. (1995). Src family protein tyrosine kinases and cellular signal transduction pathways. Curr. Opin. Cell Biol. 7, 176-182.
8. Gonfloni, S., Williams, J.C., Hattula, K., Weijland, A., Wierenga, R.K., and Superti-Furga, G. (1997). The role of the linker between the SH2 domain and catalytic domain in the regulation and function of Src. EMBO J. 16, 7261-7271.
9. Hardwick, J.S., and Sefton, B.M. (1997). The activated form of the Lck tyrosine protein kinase in cells exposed to hydrogen peroxide is phosphorylated at both Tyr-394 and Tyr-505. J. Biol. Chem. 272, 25429-25432.
10. Hubbard, S.R. (1997). Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog. EMBO J. 16, 5572-5581.
11. 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 372, 746-754.
12. Hubbard, S.R., Mohammadi, M., and Schlessinger, J. (1998). Autoregulatory mechanisms in protein-tyrosine kinases. J. Biol. Chem. 273, 11987-11990.
13. Hunter, T. (1987). A tail of two src's: mutatis mutandis. Cell 49, 1-4.
14. Jeffrey, P.D., Russo, A.A., Polyak, K., Gibbs, E., Hurwitz, J., Massague, J., and Pavletich, N.P. (1995). Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex. Nature 376, 313-320.
15. Johnson, L.N., Noble, M.E., and Owen, D.J. (1996). Active and inactive protein kinases: structural basis for regulation. Cell 85, 149-158.
16. Jones, T.A., Bergdoll, M., and Kjeldgaard, M. (1989). In Crystallographic Computing and Modeling Methods in Molecular Design, C. Bugg and S. Ealick, eds. (New York: Springer).
17. Kabsch, W. (1988). Evaluation of single crystal diffraction data from a position sensitive detector. J. Appl. Crystallogr. 21, 916-924.
18. Knighton, D.R., Zheng, J.H., Ten, E.L, Ashford, V.A., Xuong, N.H., Taylor, S.S., and Sowadski, J.M. (1991). Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253, 407-414.
19. Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
20. Krebs, E.G. (1989). The Albert Lasker medical awards. Role of the cyclic AMP-dependent protein kinase in signal transduction. JAMA 262, 1815-1818.
21. LaFevre-Bernt, M., Sicheri, F., Pico, A., Porter, M., Kuriyan, J., and Miller, W.T. (1998). Intramolecular regulatory interactions in the Src family kinase Hck probed by mutagenesis of a conserved tryptophan residue. J. Biol. Chem. 273, 32129-32134.
22. Lamzin, V.S., and Wilson, K.S. (1993). Automated refinement of protein models. Acta Crystallogr. D 49, 129-147.
23. Matsuda, M., Mayer, B.J., Fukui, Y., and Hanafusa, H. (1990). Binding of transforming protein, P47gag-crk, to a broad range of phosphotyrosine-containing proteins. Science 248, 1537-1539.
24. 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.
25. Morgan, D.O. (1995). Principles of CDK regulation. Nature 374, 131-134.
26. Morgan, D.O., and De Bondt, H.L. (1994). Protein kinase regulation: insights from crystal structure analysis. Curr. Opin. Cell Biol. 6, 239-246.
27. Navaza, J. (1992). AMoRe: a new package for molecular replacement. In Molecular Replacement: Proceedings of the CCP4 Study Weekend, E.J. Dodson, S. Gover, and W. Wolf, eds. (Daresbury, UK: SERC), pp. 87-90.
28. Otwinowski, Z. (1993). Oscillation data reduction program. In Proceedings of the CCP4 Study Weekend, L. Sawyer, N. Isaacs, and S. Burley, eds. (Daresbury, UK: SERC Daresbury Laboratory), pp. 56-62.
29. Russo, A.A., Jeffrey, P.D., and Pavletich, N.P. (1996). Structural basis of cyclin-dependent kinase activation by phosphorylation. Nat. Struct. Biol. 3, 696-700.
30. Schindler, T., Sicheri, F., Pico, A., Gazit, A., Levitzki, A., and Kuriyan, J. (1999). Crystal structure of Hck in complex with a Src family-selective tyrosine kinase inhibitor. Mol. Cell 3, this issue, 639-648.
31. Sicheri, F., Moarefi, I., and Kuriyan, J. (1997). Crystal structure of the Src family tyrosine kinase Hck. Nature 385, 602-609.
32. Superti-Furga, G., Fumagalli, S., Koegl, M., Courtneidge, S.A., and Draetta, G. (1993). Csk inhibition of c-Src activity requires both the SH2 and SH3 domains of Src. EMBO J. 12, 2625-2634.
33. Superti-Furga, G., and Courtneidge, S.A. (1995). Structure-function relationships in Src family and related protein tyrosine kinases. Bioessays 17, 321-330.
34. Taylor, S.S., Buechler, J.A., and Yonemoto, W. (1990). cAMP-dependent protein kinase: framework for a diverse family of regulatory enzymes. Annu. Rev. Biochem. 59, 971-1005.
35. Thomas, J.W., Ellis, B., Boerner, R.J., Knight, W.B., White, G.C., II, and Schaller, M.D. (1998). SH2- and SH3-mediated interactions between focal adhesion kinase and Src. J. Biol. Chem. 273, 577-583.
36. Williams, J.C., Weijland, A., Gonfloni, S., Thompson, A., Courtneidge, S.A., Superti-Furga, G., and Wierenga, R.K. (1997). The 2.35 Å crystal structure of the inactivated form of chicken Src: a dynamic molecule with multiple regulatory interactions. J. Mol. Biol. 274, 757-775.
37. Xu, W., Harrison, S.C., and Eck, M.J. (1997). Three-dimensional structure of the tyrosine kinase c-Src. Nature 385, 595-602.
38. Yamaguchi, H., and Hendrickson, W.A. (1996). Structural basis for activation of the human lymphocyte kinase Lck upon tyrosine phosphorylation. Nature 384, 484-489.
39. Zheng, J., Knighton, D.R., ten Eyck, L.F., Karlsson, R., Xuong, N., Taylor, S.S., and Sowadski, J.M. (1993). Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor. Biochemistry 32, 2154-2161.