Structure and ligand recognition of the phosphotyrosine binding domain of Shc

Nature

Volumn 378, Issue 6557, 1995, Pages 584-592

  Zhou, Ming Ming ^a   Ravichandran, Kodimangalam S ^b   Olejniczak, Edward T ^a   Petros, Andrew M ^a   Meadows, Robert P ^a   Sattler, Michael ^a   Harlan, John E ^a   Wade, Warren S ^a   Burakoff, Steven J ^b   Fesik, Stephen W ^a  

^a ABBOTT LABORATORIES   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

LIGAND; NERVE GROWTH FACTOR RECEPTOR; PHOSPHOLIPID; PHOSPHOPEPTIDE; PHOSPHOTYROSINE; PROTEIN; TYROSINE;

ARTICLE; BINDING SITE; LIGAND BINDING; MEMBRANE; MOLECULAR RECOGNITION; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; BINDING SITES; BLOOD PROTEINS; LIGANDS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PHOSPHOLIPIDS; PHOSPHOPEPTIDES; PHOSPHOTYROSINE; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEINS; PROTO-ONCOGENE PROTEINS; RECEPTOR PROTEIN-TYROSINE KINASES; RECEPTOR, TRKA; RECEPTORS, NERVE GROWTH FACTOR; SIGNAL TRANSDUCTION; SRC HOMOLOGY DOMAINS; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, P.H.S.;

EID: 0028860968     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/378584a0     Document Type: Article

References (50)

1. Giorgetti, S., Pelicci, P. G., Pelicci, G. & Van Obberghen, E. Eur. J. Biochem. 223,195-202 (1994).
2. Pelicci, G. et al. Cell 70, 93-104 (1992).
3. Rozakis-Adcock, M. et al. Nature 360, 689-692 (1992).
4. Stephens, R. M. et al, Neuron 12, 691-705 (1994).
5. Obermeier, A. et al. EMBO J. 13, 1585-1590 (1994).
6. Ravichandran, K. S. & Burakoff, S. J. J. biol. Chem. 269, 1599-1602 (1993).
7. Burns, L. A., Karnitz, L. M., Sutor, S. L. & Abraham, R. T. J. biol. Chem. 268,17659-17661 (1993).
8. Sato, N., Sakamaki, K., Terada, N., Arai, K. & Miyajima, A. EMBOJ. 12, 4181-4189 (1993).
9. Ravichandran, K. S. et al. Science 262, 902-905 (1993).
10. Saxton, T., van Oostveen, I., Bowtell, D., Aebersold, R. & Gold, M. J. Immun. 153, 623-636 (1994).
11. Egan, S. E. Nature 363, 45-51 (1993).
12. Van Biesen, T. et al. Nature 376, 781-784 (1995).
13. Lev, S. et al. Nature 376, 737-745 (1995).
14. Kavanaugh, W. M. & Williams, L. T. Science 266,1862-1865 (1994).
15. Blaikie, P. et al. J. biol. Chem. 269, 32031-32034 (1994).
16. Gustafson, T. A., He, W., Craparo, A., Schaub, C. D. & O’Neill, T. J. Molec. cell. Biol. 15, 2500-2508 (1995).
17. Songyang, Z. et al. Molec. cell. Biol. 14, 2777-2785 (1994).
18. Songyang, Z., Margolis, B., Chaudhur, M., Shoelson, S. E. & Cantley, L. C. J. biol. Chem. 270, 14863-14866 (1995).
19. Trüb, T. et al. J. biol. Chem. 270, 18205-18208 (1995).
20. Kavanaugh, W. M., Turck, C. W. & Williams, L. T. Science 268, 1177-1179 (1995).
21. Van der Geer, P. et al. Curr. Biol. 5, 404-412 (1995).
22. Zhou, M.-M. et al. J. biol. Chem. 270, 31119-31123 (1995).
23. Dikic, I. et al. J. biol. Chem. 270, 15125-15129 (1985).
24. O’Neill, T. J., Craparo, A. & Gustafson, T. A. Molec. cell. Biol. 14, 6433-6442 (1994).
25. Bork, P. & Margolis, B. Cell 80, 693-694 (1995).
26. Sun, X. J. et al. Nature 377, 173-177 (1995).
27. Vamazaki, T., Lee, W., Arrowsmith, C. H., Muhandiram, D. R. & Kay, L. E. J. Am. chem. Soc. 116, 11655-11666 (1994).
28. Nilges, M., Clore, G. M. & Gronenborn, A. M. FEBS Lett. 229, 317-324 (1988).
29. Kuszewski, J., Nilges, M. & Brünger, A. T. J. biomolec. NMR 2, 33-56 (1992).
30. Wilmot, C. M. & Thornton, J. M. J. molec. Biol. 203, 221-232 (1988).
31. Bansal, A. & Gierasch, L. M. Cell 67, 1195-1201 (1991).
32. Eck, M. J., Shoelson, S. E., & Harrison, S. C. Nature 362, 87-91 (1993).
33. Waksman, G., Shoelson, S. E., Pant, N., Cowburn, D. & Kuriyan, J. Cell 72, 779-790 (1993).
34. Zhou, M.-M. et al. Proc. natn. Acad. Sei. U.S.A. 92, 7784-7788 (1995).
35. Flower, D. R. FEBS Lett. 333, 99-102 (1993).
36. Saraste, M. & Hyvönen, M. Curr. Opin. struct. Biol. 5, 403-408 (1995).
37. Musacchio, A. et al. Trends biochem. Sei. 18, 343-348 (1993).
38. Touhara, K. et al. J. biol. Chem. 269, 10217-10220 (1994).
39. Harlan, J. E., Hajduk, P. J., Voon, H. S. & Fesik, S. W. Nature 371, 168-170 (1994).
40. Silvius, J. R. & l’Heureax, F. Biochemistry 33, 3014-3022 (1994).
41. Peitzsch, R. M. & Mclaughlin, S. Biochemistry 32, 10436-10443 (1993).
42. Brooks, B. R. et al. J. comput. Chem. 4, 187-217 (1983).
43. Carson, M. J. molec. Graph. 5, 103-106 (1987).
44. Clore, G. M. & Gronenborn, A. M. Meth. Enzym. 239, 349-363 (1994).
45. Brünger, A. T. X-PLOR Manual, version 3.1 (Yale Univ. Press, Cambridge, MA, 1992).
46. Kuboniwa, H., Grzesiek, S., Delaglio, F. & Bax, A. J. biomolec. NMR 4, 871-878 (1994).
47. Yoon, H. S. et al. Nature 369, 672-675 (1994).
48. Hope, M. J., Bally, M. B., Webb, G. & Cullis, P. R. Biochim. biophys. Acta 812, 55-65 (1985).
49. Tortorella, D. & London, E. Analyt. Biochem. 217, 176-180 (1994).
50. Rebecchi, M., Peterson, A. & McLaughlin, S. Biochemistry 31, 12742-12747 (1992).