Three-dimensional structure of the tyrosine kinase c-Src

Nature

Volumn 385, Issue 6617, 1997, Pages 595-602

  Xu, Wenqing ^a   Harrison, Stephen C ^b,c   Eck, Michael J ^b  

^a BOSTON CHILDREN S HOSPITAL   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

^c HOWARD HUGHES MEDICAL INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN KINASE P60; PROTEIN TYROSINE KINASE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; ENZYME ACTIVITY; ENZYME STRUCTURE; ONCOGENE SRC; PRIORITY JOURNAL; PROTEIN DOMAIN; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; ENZYME ACTIVATION; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTO-ONCOGENE PROTEINS PP60(C-SRC); SRC HOMOLOGY DOMAINS;

EID: 0031025991     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/385595a0     Document Type: Article

References (52)

1. Bishop, J. Viral Oncogenes. Cell 42, 23-28 (1985).
2. Brown, M. T. & Cooper, J. A. Regulation, substrates and functions of sec. Biochim. Biophys. Acta 1287, 121-149 (1996).
3. Superti-Furga, G. & Courtneidge, S. A. Structure-function relationships in Src family and related protein tyrosine kinases. Bioessays 17, 321-330 (1995).
4. Pawson, T. Protein modules and signalling networks. Nature 373, 573-580 (1995).
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).
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).
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).
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).
9. Songyang, Z et al. SH2 domains recognize specific phosphopeptide sequences. Cell 72, 767-778 (1993).
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).
11. lck. Nature 362, 87-91 (1993).
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).
13. Hunter, T. A tail of two src's: mutatis mutandis. Cell 49, 1-4 (1987).
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).
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).
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).
17. Cooper, J. A. & Howell, B. The when and how of Src regulation. Cell 73, 1051-1054 (1993).
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).
19. Ellis, B. et al. Purification and characterization of deletional mutations of pp60c-src tyrosine kinase. J. Cell. Biochem. (suppl.) 18B, 276 (1994).
20. Knighton, D. R. et al. Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253, 407-414 (1991).
21. Madhusudan et al. cAMP-dependent protein kinase: crystallographic insights into substrate recognition and phosphotransfer. Protein Sci. 3, 176-187 (1994).
22. De Bondt, H. L. et al. Crystal structure of cyclin-dependent kinase 2. Nature 363, 595-602 (1993).
23. Jeffrey, P. D. et al. Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex. Nature 376, 313-320 (1995).
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).
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).
26. Johnson, L. N., Noble, M. E. & Owen, D. J. Active and inactive protein kinases: structural basis for regulation. Cell 85, 149-158 (1996).
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).
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).
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).
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).
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).
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).
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).
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 p561ck 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).
36. Yamagushi, H. & Hendrickson, W. A. Structural basis for activation of the human lymphocyte kinase Lck upon tyrosine phosphorylation. Nature 384, 484-489 (1996).
37. Sicheri, F., Moarefi, I. & Kuriyan, J. Nature 385, 602-609 (1997).
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).
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).
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).
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 lyrosine. J. Biol. Chem. 268, 18070-18075 (1993).
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).
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).
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).
45. Kabsch, W. Evaluation of single crystal diffraction data from a position sensitive detector. J. Appl. Crystallogr. 21, 916-924 (1988).
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, New York, 1989).
48. Brunger, A. T. X-PLOR Version 3.0: A System for Crystallography and NMR (Yale University Press, New Haven, CT, 1992).
49. Lamzin, V. S. & Wilson, K. S. Automated refinement of protein models. Acta Crystallogr. D 49, 129-147 (1993).
50. Kraulis, P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
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).
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).