Structure of the N-terminal SH3 domain of GRB2 complexed with a peptide from the guanine nucleotide releasing factor Sos (original) (raw)

References

  1. Mayer, B.J. & Baltimore, D. Signaling through SH2 and SH3 domains. Trends Cell Biol. 3, 8–13 (1993).
    Article CAS Google Scholar
  2. Pawson, T. & Schlessinger, J. SH2 and SH3 domains. Curr. Biol. 3, 434–442 (1993).
    Article CAS Google Scholar
  3. Kuriyan, J. & Cowburn, D. Structures of SH2 and SH3 domains. Curr. Opin. struct. Biol. 3, 828–837 (1993).
    Article CAS Google Scholar
  4. Cicchetti, P., Mayer, B.J., Thiel, G. & Baltimore, D. Identification of a protein that binds to the SH3 region of Abl and is similar to Bcr and GAP-rho. Science 257, 803–806 (1992).
    Article CAS Google Scholar
  5. Bar-sagi, D., Rotin, D., Batzer, A., Mandiyan, V. & Schlessinger, J. SH3 domains direct cellular localization of signaling molecules. Cell 74, 83–91 (1993).
    Article CAS Google Scholar
  6. Musacchio, A., Noble, M., Pauptit, R., Wierenga, R. & Saraste, M. Crystal structure of a Src-homology 3 (SH3) domain. Nature 359, 851–855(1992).
    Article CAS Google Scholar
  7. Yu, H. et al. Solution structure of the SH3 domain of Src and identification of its ligand-binding site. Science 258, 1665–1668 (1992).
    Article CAS Google Scholar
  8. Kohda, D. et al. Solution structure of the SH3 domain of phospholipase C-γ. Cell 72, 953–960 (1993).
    Article CAS Google Scholar
  9. Koyama, S. et al. Structure of the P13K SH3 domain and analysis of the SH3 family. Cell 72, 945–952 (1993).
    Article CAS Google Scholar
  10. Booker, G.W. et al. Solution structure and ligand-binding site of the SH3 domain of the p85α subunit of phosphatidylinositol 3-kinase. Cell 73, 813–822 (1993).
    Article CAS Google Scholar
  11. Noble, M.E.M., Musacchio, A., Saraste, M., Courtneidge, S.A. & Wierenga, R.K. Crystal structure of the SH3 domain in human Fyn; comparison of the three-dimensional structures of SH3 domains in tyrosine kinases and spectrin. EMBO J. 12, 2617–2624 (1993).
    Article CAS Google Scholar
  12. Borchert, T.V., Mathieu, M., Zeelen, J.P., Courtneidge, S.A. & Wierenga, R.K. The crystal structure of human Csk SH3: structural diversity near the RT-Src and n-Src loop. FFBS Letts 341, 79–85 (1994).
    Article CAS Google Scholar
  13. Yang, Y.S. et al. Solution structure of GAP SH3 domain by 1H NMR and spatial arrangement of essential Ras signaling-involved sequence. EMBO J. 13, 1270–1279 (1994).
    Article CAS Google Scholar
  14. 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 368, 764–769(1994).
    Article CAS Google Scholar
  15. Kohda, D. et al. Solution structure and ligand-binding site of the C-terminal SH3 domain of GRB2. Structure in the press (1994).
    Google Scholar
  16. Yu, H. et al. Structural basis for the binding of proline-rich peptides to SH3 domains. Cell 76, 933–945 (1994).
    Article CAS Google Scholar
  17. Musacchio, A., Saraste, M. & Wilmanns, M. High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides. Nature struct. Biol. 1, 546–551 (1994).
    Article CAS Google Scholar
  18. Lowenstein, E.J. et al. The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to Ras signaling. Cell 70, 431–442 (1992).
    Article CAS Google Scholar
  19. Clark, S.G., Stern, M.J. & Horvitz, H.R. C. elegans cell-signalling gene sem-5 encodes a protein with SH2 and SH3 domains. Nature 356, 340–344 (1992).
    Article CAS Google Scholar
  20. Marshall, C.J. MAP kinase kinase kinase, MAP kinase kinase and MAP kinase. Curr. Opin. Gen. Dev. 4, 82–89 (1994).
    Article CAS Google Scholar
  21. Batzer, A.G., Rotin, D., Urena, J.M., Skolnik, E.Y. & Schlessinger, J. Hierarchy of binding sites for Grb2 and Shc on the epidermal growth factor receptor. Molec. Cell Biol. 14, 5192–5201 (1994).
    Article CAS Google Scholar
  22. White, M.F. The IRS-1 signaling system. Curr. Opin. Gen. Dev. 4, 47–54 (1994).
    Article CAS Google Scholar
  23. Skolnik, E.Y. et al. Function of protein GRB2 in linking the insulin receptor to ras signaling pathways. Science 260, 1953–1955 (1993).
    Article CAS Google Scholar
  24. Bowtell, D. Fu, P., Simon, M. & Senior, P. Identification of murine homologs of the Drosophila Son of sevenless gene: potential activators of ras. Proc. natn. Acad. Sci. U.S.A. 89, 6511–6515 (1992).
    Article CAS Google Scholar
  25. Brünger, A.T. X-PLOR Version 3.1: A System for X-ray Crystallography and NMR, (Yale University Press, New Haven, CT; 1992).
    Google Scholar
  26. Sasisekharan, V. Structure of poly-L-proline II. Acta crystallogr. 12, 897–909 (1959).
    Article CAS Google Scholar
  27. Adzhubei, A.A. & Sternberg, M.J.E. Left-handed polyproline II helices commonly occur in globular proteins. J. molec. Biol. 229, 472–493 (1993).
    Article CAS Google Scholar
  28. Lim, W.A. & Richards, F.M. Critical residues in an SH3 domain from Sem-5 suggest a mechanism for proline-rich peptide recognition. Nature struct. Biol. 1, 221–225 (1994).
    Article CAS Google Scholar
  29. Chen, J.K., Lane, W.S., Brauer, A.W., Tanaka, A. & Schreiber, S.L. Biased combinatorial libraries: novel ligands for the SH3 domain of phosphatidylinositol 3-kinase. J. Am. chem. Soc. 115, 12591–12592 (1993).
    Article CAS Google Scholar
  30. Gout, I. et al. The GTPase dynamin binds to and is activated by a subset of SH3 domains. Cell 75, 25–36 (1993).
    Article CAS Google Scholar
  31. Studier, F.W. & Moffatt, B.A. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. molec. Biol. 189, 113–130 (1986).
    Article CAS Google Scholar
  32. Rance, M. et al. Improved spectral resolution in COSY 1H NMR spectra of proteins via double quantum filtering. Biochem. biophys. Res. Commun. 117, 479–485 (1983).
    Article CAS Google Scholar
  33. Bax, A. & Davis, D.G. MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. magn. Reson. 65, 355–360 (1985).
    CAS Google Scholar
  34. Müller, L. P.E. COSY, a simple alternative to E.COSY. J. magn. Reson. 72, 191–196 (1987).
    Google Scholar
  35. Macura, S., Huang, Y., Suter, D. & Ernst, R.R. Two-dimensional chemical exchange and cross-relaxation spectroscopy of coupled nuclear spins. J. magn. Reson. 43, 259–281 (1981).
    CAS Google Scholar
  36. States, D.J., Haberkorn, R.A. & Ruben, D.J. A two-dimensional nuclear Overhauser experiments with pure absorption phase in four quadrants. J. magn. Reson. 48, 286–292 (1982).
    CAS Google Scholar
  37. Bodenhausen, G. & Ruben, D.J. Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy. Chem. Phys. Lett. 69, 185–189 (1980).
    Article CAS Google Scholar
  38. Norwood, T.J., Boyd, J., Heritage, J.E., Soffe, N. & Campbell, I.D. Comparison of techniques for 1H-detected heteronuclear 1H-15N spectroscopy. J. magn. Reson. 87, 488–501 (1990).
    CAS Google Scholar
  39. Kay, L.E., Keifer, P. & Saarinen, T. Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. chem. Soc. 114, 10663–10665 (1992).
    Article CAS Google Scholar
  40. Ikura, M. et al. Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science 256, 632–638 (1992).
    Article CAS Google Scholar
  41. Kay, L.E. & Bax, A. New methods for the measurements of NH-CαH coupling constants in 15N-labeled proteins. J. magn. Reson.. 86, 110–126 (1990).
    CAS Google Scholar
  42. Wüthrich, K. NMR of Proteins and Nucleic Acids, (John Wiley and Sons, New York, NY; 1986).
    Book Google Scholar
  43. Suri, A.K. & Levy, R.M. Estimation of interatomic distances in proteins from NOE spectra at longer mixing times using an empirical two-spin equation. J. magn. Reson. B101, 320–324 (1993).
    Article Google Scholar
  44. Hatanaka, H. et al. Tertiary structure of erabutoxin b in aqueous solution as elucidated by two-dimensional nuclear magnetic resonance. J. molec. Biol. 240, 155–166 (1994).
    Article CAS Google Scholar
  45. Kraulis, P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structure. J. appl. Crystallogr. 24, 946–950 (1991).
    Article Google Scholar
  46. Brooks, B.R. et al. CHARMM:a program for macromolecular energy, minimization, and dynamics calculation. J. comput. Chem. 4, 187–217 (1983).
    Article CAS Google Scholar

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