Three-dimensional structure of the tyrosine kinase c-Src (original) (raw)

References

1. Bishop, J. Viral Oncogenes. Cell 42, 23–28 (1985).
   Article CAS PubMed Google Scholar
2. Brown, M. T. & Cooper, J. A. Regulation, substrates and functions of sec. Biochim. Biophys. Acta 1287, 121–149 (1996).
   PubMed Google Scholar
3. Superti-Furga, G. & Courtneidge, S. A. Structure-function relationships in Src family and related protein tyrosine kinases. Bioessays 17, 321–330 (1995).
   Article CAS PubMed Google Scholar
4. Pawson, T. Protein modules and signalling networks. Nature 373, 573–580 (1995).
   Article ADS CAS PubMed Google Scholar
5. Yu, H. et al. Solution structure of the SH3 domain and Src and identification of its ligand-binding site. Science 258, 1665–1668 (1992).
   Article ADS CAS PubMed Google Scholar
6. Musacchio, A., Saraste, M. & Willmanns, M. High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides. Nature Struct. Biol. 1, 546–551 (1994).
   Article CAS PubMed Google Scholar
7. Ren, R., Mayer, B. J., Cicchetti, P. & Baltimore, D. Identification of a ten amino acid proline-rich SH3 binding site. Science 259, 1157–1161 (1993).
   Article ADS CAS PubMed Google Scholar
8. Mayer, B. J., Jackson, P. K. & Baltimore, D. The noncatalytic src homology region 2 segment of abl tyrosine kinase binds to tyrosine-phosphorylated cellular proteins with high affinity. Proc. Natl Acad. Sci. USA 88, 627–631 (1991).
   Article ADS CAS PubMed PubMed Central Google Scholar
9. Songyang, Z et al. SH2 domains recognize specific phosphopeptide sequences. Cell 72, 767–778 (1993).
   Article CAS PubMed Google Scholar
10. Waksman, G., Shoelson, S. E., Pant, N., Cowburn, D. & Kuriyan, J. Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms. Cell 72, 779–790 (1993).
    Article CAS PubMed Google Scholar
11. Eck, M. J., Shoelson, S. E. & Harrison, S. C. Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56_lck_. Nature 362, 87–91 (1993).
    Article ADS CAS PubMed Google Scholar
12. Takeya, T. & Hanafusa, H. Structure and sequence of the cellular gene homologous to the RSV src gene and the mechanism for generating the transforming virus. Cell 32, 881–890 (1983).
    Article CAS PubMed Google Scholar
13. Hunter, T. A tail of two src's: mutatis mutandis. Cell 49, 1–4 (1987).
    Article CAS PubMed Google Scholar
14. Nada, S., Okada, M., MacAuley, A., Cooper, J. A. & Nakagawa, H. Cloning of a complementary DNA for a protein-tyrosine kinase that specifically phosphorylates a negative regulatory site of p60c-src. Nature 351, 69–72 (1991).
    Article ADS CAS PubMed Google Scholar
15. Matsuda, M., Mayer, B. J., Fukui, Y. & Hanafusa, H. Binding of transforming protein, P47gag-crk, to a broad range of phosphotyrosine-containing proteins. Science 248, 1537–1539 (1990).
    Article ADS CAS PubMed Google Scholar
16. Roussel, R. R., Brodeur, S. R., Shalloway, D. & Laudano, A. P. Selective binding of activated pp60c-src by an immobilized synthetic phosphopeptide modeled on the carboxyl terminus of pp60c-src. Proc. Natl Acad. Sci. USA 88, 10696–10700 (1991).
    Article ADS CAS PubMed PubMed Central Google Scholar
17. Cooper, J. A. & Howell, B. The when and how of Src regulation. Cell 73, 1051–1054 (1993).
    Article CAS PubMed Google Scholar
18. Koegl, M., Courtneidge, S. A. & Superti-Furga, G. Structural requirements for the efficient regulation of the Src protein tyrosine kinase by Csk. Oncogene 11, 2317–2329 (1995).
    CAS PubMed Google Scholar
19. Ellis, B. et al. Purification and characterization of deletional mutations of pp60c-src tyrosine kinase. J. Cell. Biochem. (suppl.) 18B, 276 (1994).
    Google Scholar
20. Knighton, D. R. et al. Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253, 407–414 (1991).
    Article ADS CAS PubMed Google Scholar
21. Madhusudan et al. CAMP-dependent protein kinase: crystallographic insights into substrate recognition and phosphotransfer. Protein Sci. 3, 176–187 (1994).
    Article CAS PubMed PubMed Central Google Scholar
22. De Bondt, H. L. et al. Crystal structure of cyclin-dependent kinase 2. Nature 363, 595–602 (1993).
    Article ADS CAS PubMed Google Scholar
23. Jeffrey, P. D. et al. Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex. Nature 376, 313–320 (1995).
    Article ADS CAS PubMed Google Scholar
24. Hubbard, S. R., Wei, L., Ellis, L. & Hendrickson, W. A. Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature 372, 746–754 (1994).
    Article ADS CAS PubMed Google Scholar
25. Mohammadi, M., Schlessinger, J. & Hubbard, S. R. Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism. Cell 86, 577–587 (1996).
    Article CAS PubMed Google Scholar
26. Johnson, L. N., Noble, M. E. & Owen, D. J. Active and inactive protein kinases: structural basis for regulation. Cell 85, 149–158 (1996).
    Article CAS PubMed Google Scholar
27. Kato, J. Y. et al. Amino acid substitutions sufficient to convert the nontransforming p60c-src protein to a transforming protein. Mol. Cell. Biol. 6, 4155–4160 (1986).
    Article CAS PubMed PubMed Central Google Scholar
28. Potts, W. M., Reynolds, A. B., Lansing, T. J. & Parsons, J. T. Activation of pp60c-src transforming potential by mutations altering the structure of an amino terminal domain containing residues 90-95. Oncogene Res. 3, 343–355 (1988).
    CAS PubMed Google Scholar
29. Superti-Furga, G., Fumagalli, S., Koegl, M., Courtneidge, S. A. & Draetta, G. Csk inhibition of c-Src activity requires both the SH2 and SH3 domains of Src. EMBO J. 12, 2625–2634 (1993).
    Article CAS PubMed PubMed Central Google Scholar
30. Levy, J. B. & Brugge, J. S. Biological and biochemical properties of the c-src+ gene product overexpressed in chicken embryo fibroblasts. Mol. Cell. Biol. 9, 3332–3341 (1989).
    Article CAS PubMed PubMed Central Google Scholar
31. Feng, S., Chen, J. K., Yu, H., Simon, J. A. & Schreiber, S. L. Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactions. Science 266, 1241–1247 (1994).
    Article ADS CAS PubMed Google Scholar
32. Lim, W. A., Richards, F. M. & Fox, R. O. Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains. Nature 372, 375–379 (1994).
    Article ADS CAS PubMed Google Scholar
33. Eck, M. J., Atwell, S. K., Shoelson, S. E. & Harrison, S. C. Structure of the regulatory domains of the Src-family tyrosine kinase Lck. Nature 268, 764–769 (1994).
    Article ADS Google Scholar
34. Kuriyan, J. & Cowburn, D. Modular peptide recognition domains in eukaryotic signaling. Annu. Rev. Biophys. Biomol. Struct. (in the press).
35. Payne, G., Shoelson, S. E., Gish, G. D., Pawson, T. & Walsh, C. T. Kinetics of p56lck and p60src Src homology 2 domain binding to tyrosine-phosphorylated peptides determined by a competition assay or surface plasmon resonance. Proc. Natl Acad. Sci. USA 90, 4902–4906 (1993).
    Article ADS CAS PubMed PubMed Central Google Scholar
36. Yamagushi, H. & Hendrickson, W. A. Structural basis for activation of the human lymphocyte kinase Lck upon tyrosine phosphorylation. Nature 384, 484–489 (1996).
    Article ADS Google Scholar
37. Sicheri, F., Moarefi, I. & Kuriyan, J. Nature 385, 602–609 (1997).
    Article ADS CAS PubMed Google Scholar
38. Boerner, R. J. et al. 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 (1996).
    Article CAS PubMed Google Scholar
39. Levy, J. B., Iba, H. & Hanafusa, H. Activation of the transforming potential of p60c-src by a single amino acid change. Proc. Natl Acad. Sci. USA 83, 4228–4232 (1986).
    Article ADS CAS PubMed PubMed Central Google Scholar
40. Murphy, S. M., Bergman, M. & Morgan, D. O. Suppression of c-Src activity by C-terminal Src kinase involves the c-Src SH2 and SH3 domains: analysis with Saccharomyces cerevisiae. Mol. Cell. Biol. 13, 5290–5300 (1993).
    Article CAS PubMed PubMed Central Google Scholar
41. Okada, M., Howell, B. W., Broome, M. A. & Cooper, J. A. Deletion of the SH3 domain of Src interferes with regulation by the phosphorylated carboxyl-terminal tyrosine. Biol. Chem. 268, 18070–18075 (1993).
    CAS Google Scholar
42. Erpel, T., Superti-Furga, G. & Courtneidge, S. A. Mutational analysis of the Src SH3 domain: the same residues of the ligand binding surface are important for intra- and intermolecular interactions. EMBO J. 14, 963–975 (1995).
    Article CAS PubMed PubMed Central Google Scholar
43. Haystead, C. M., Gregory, P., Sturgill, T. W. & Haystead, T. A. Gamma-phosphate-linked ATP- sepharose for the affinity purification of protein kinases. Rapid purification to homogeneity of skeletal muscle mitogen-activated protein kinase kinase. Eur. J. Biochem. 214, 459–467 (1993).
    Article CAS PubMed Google Scholar
44. Otwinowski, Z. in Proceedings of the CCP4 Study Weekend (eds Sawyer, L., Isaacs, N. & Burley, S.) 56–62 (SERC Daresbury Laboratory, Daresbury, UK, 1993).
    Google Scholar
45. Kabsch, W. Evaluation of single crystal diffraction data from a position sensitive detector. J. Appl. Crystallogr. 21, 916–924 (1988).
    Article CAS Google Scholar
46. Collaborative Computational Project Number 4. The CCP4 suite: Programs for protein crystallography. Acta Crystallogr. D 50, 760–776 (1994).
47. Jones, T. A., Bergdoll, M. & Kjeldgaard, M. in Crystallographic Computing and Modeling Methods in Molecular Design (eds Bugg, C. & Ealick, S.) (Springer, NewYork, 1989).
    Google Scholar
48. Brunger, A. T. X-PLOR Version 3.0: A System for Crystallography and NMR (Yale University Press, New Haven, CT, 1992).
    Google Scholar
49. Lamzin, V. S. & Wilson, K. S. Automated refinement of protein models. Acta Crystallogr. D 49, 129–147 (1993).
    Article CAS PubMed Google Scholar
50. Kraulis, P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946–950 (1991).
    Article Google Scholar
51. Nicholls, A., Sharp, K. A. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet. 11, 281–296 (1991).
    Article CAS PubMed Google Scholar
52. Alexandropoulos, K. & Baltimore, D. Coordinate activation of c-Src by SH3- and SH2-binding sites on a novel p130Cas-related protein, Sin. Genes Dev. 10, 1341–1355 (1996).
    Article CAS PubMed Google Scholar

Download references