Structure of the interleukin-2 tyrosine kinase Src homology 2 domain; Comparison between X-ray and NMR-derived structures

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Volumn 68, Issue 2, 2012, Pages 145-153

  Joseph, Raji E ^a   Ginder, Nathaniel D ^a   Hoy, Julie A ^b   Nix, Jay C ^c   Fulton, D Bruce ^a   Honzatko, Richard B ^a   Andreotti, Amy H ^a  

^a IOWA STATE UNIVERSITY   (United States)

^b California Institute of Technology   (United States)

^c LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

Author keywords

domain swapping; IL 2 inducible T cell kinase; proline isomerization; Src homology 2 domain

Indexed keywords

EMT PROTEIN TYROSINE KINASE; EMT PROTEIN-TYROSINE KINASE; PROTEIN TYROSINE KINASE;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; GENETICS; MOLECULAR GENETICS; MOUSE; MUTATION; NUCLEAR MAGNETIC RESONANCE; PROTEIN QUATERNARY STRUCTURE; SRC HOMOLOGY DOMAIN; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; ANIMALS; CRYSTALLOGRAPHY, X-RAY; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN STRUCTURE, QUATERNARY; PROTEIN-TYROSINE KINASES; SRC HOMOLOGY DOMAINS;

EID: 84856844918     PISSN: None     EISSN: 17443091     Source Type: Journal    
DOI: 10.1107/S1744309111049761     Document Type: Article

References (44)

1. Adams, P. D. et al. (2010). Acta Cryst. D66, 213-221.
2. Andreotti, A. H. (2003). Biochemistry, 42, 9515-9524.
3. Brazin, K. N., Fulton, D. B. & Andreotti, A. H. (2000). J. Mol. Biol. 302, 607-623.
4. Brazin, K. N., Mallis, R. J., Fulton, D. B. & Andreotti, A. H. (2002). Proc. Natl Acad. Sci. USA, 99, 1899-1904.
5. Breheny, P. J., Laederach, A., Fulton, D. B. & Andreotti, A. H. (2003). J. Am. Chem. Soc. 125, 15706-15707.
6. Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J.-S., Kuszewski, J., Nilges, M., Pannu, N. S., Read, R. J., Rice, L. M., Simonson, T. & Warren, G. L. (1998). Acta Cryst. D54, 905-921.
7. Colgan, J., Asmal, M., Neagu, M., Yu, B., Schneidkraut, J., Lee, Y., Sokolskaja, E., Andreotti, A. & Luban, J. (2004). Immunity, 21, 189-201.
8. DeLano, W. L. (2002). PyMOL. http://www.pymol.org.
9. Demeler, B. (2005). Analytical Ultracentrifugation, edited by D. J. Scott, S. E. Harding & A. J. Rowe, pp. 210-230. Cambridge: Royal Society of Chemistry.
10. Eckert, B., Martin, A., Balbach, J. & Schmid, F. X. (2005). Nature Struct. Mol. Biol. 12, 619-623.
11. Fischer, G. & Aumüller, T. (2003 Rev. Physiol. Biochem. Pharmacol. 148, 105-150.
12. French, S. & Wilson, K. (1978). Acta Cryst. A34, 517-525.
13. Frese, S., Schubert, W. D., Findeis, A. C., Marquardt, T., Roske, Y. S., Stradal, T. E. & Heinz, D. W. (2006). J. Biol. Chem. 281, 18236-18245.
14. Jones, T. A., Zou, J.-Y., Cowan, S. W. & Kjeldgaard, M. (1991). Acta Cryst. A47, 110-119.
15. Joseph, R. E., Ginder, N. D., Hoy, J. A., Nix, J. C., Honzatko, R. B. & Andreotti, A. H. (2011). Acta Cryst. F67, 269-273.
16. Kabsch, W. (1976). Acta Cryst. A32, 922-923.
17. Koo, B.-K., Park, C.-J., Fernandez, C. F., Chim, N., Ding, Y., Chanfreau, G. & Feigon, J. (2011). J. Mol. Biol. 411, 927-942.
18. Laue, T. M., Shah, B. D., Ridgeway, T. M. & Pelletier, S. L. (1992). Analytical Ultracentrifugation in Biochemistry and Polymer Science, edited by S. E. Harding, A. J. Rowe & J. C. Horton, pp. 90-125. Cambridge: Royal Society of Chemistry.
19. Lu, K. P. (2000). Prog. Cell Cycle Res. 4, 83-96.
20. Lummis, S. C., Beene, D. L., Lee, L. W., Lester, H. A., Broadhurst, R. W. & Dougherty, D. A. (2005). Nature (London), 438, 248-252.
21. Mallis, R. J., Brazin, K. N., Fulton, D. B. & Andreotti, A. H. (2002). Nature Struct. Biol. 9, 900-905.
22. Marengere, L. E. & Pawson, T. (1994). J. Cell Sci. Suppl. 18, 97-104.
23. McCoy, A. J., Grosse-Kunstleve, R. W., Storoni, L. C. & Read, R. J. (2005). Acta Cryst. D61, 458-464.
24. McRee, D. E. (1999). J. Struct. Biol. 125, 156-165.
25. Min, L., Wu, W., Joseph, R. E., Fulton, D. B., Berg, L. & Andreotti, A. H. (2010). J. Immunol. 184, 4228-4235.
26. Murshudov, G. N., Skubák, P., Lebedev, A. A., Pannu, N. S., Steiner, R. A., Nicholls, R. A., Winn, M. D., Long, F. & Vagin, A. A. (2011). Acta Cryst. D67, 355-367.
27. Nelson, C. J., Santos-Rosa, H. & Kouzarides, T. (2006). Cell, 126, 905-916.
28. OuYang, B., Pochapsky, S. S., Dang, M. & Pochapsky, T. C. (2008). Structure, 16, 916-923.
29. Pastorino, L., Sun, A., Lu, P.-J., Zhou, X. Z., Balastik, M., Finn, G., Wulf, G., Lim, J., Li, S.-H., Li, X., Xia,W., Nicholson, L. K. & Lu, K. P. (2006). Nature (London), 440, 528-534.
30. Pflugrath, J. W. (1999). Acta Cryst. D55, 1718-1725.
31. Pletneva, E. V., Sundd, M., Fulton, D. B. & Andreotti, A. H. (2006). J. Mol. Biol. 357, 550-561.
32. Read, R. J. (2001). Acta Cryst. D57, 1373-1382.
33. Sarkar, P., Reichman, C., Saleh, T., Birge, R. B. & Kalodimos, C. G. (2007). Mol. Cell, 25, 413-426.
34. Sarkar, P., Saleh, T., Tzeng, S. R., Birge, R. B. & Kalodimos, C. G. (2011). Nature Chem. Biol. 7, 51-57.
35. Schiering, N., Casale, E., Caccia, P., Giordano, P. & Battistini, C. (2000). Biochemistry, 39, 13376-13382.
36. Severin, A., Joseph, R. E., Boyken, S., Fulton, D. B. & Andreotti, A. H. (2009). J. Mol. Biol. 387, 726-743.
37. Stein, N. (2008). J. Appl. Cryst. 41, 641-643.
38. Storoni, L. C., McCoy, A. J. & Read, R. J. (2004). Acta Cryst. D60, 432-438.
39. Strong, M., Sawaya, M. R., Wang, S., Phillips, M., Cascio, D. & Eisenberg, D. (2006). Proc. Natl Acad. Sci. USA, 103, 8060-8065.
40. Terwilliger, T. C. (2000). Acta Cryst. D56, 965-972.
41. Terwilliger, T. C. & Berendzen, J. (1999). Acta Cryst. D55, 849-861.
42. Waksman, G., Kominos, D., Robertson, S. C., Pant, N., Baltimore, D., Birge, R. B., Cowburn, D., Hanafusa, H., Mayer, B. J., Overduin, M., Resh, M. D., Rios, C. B., Silverman, L. & Kuriyan, J. (1992). Nature (London), 358, 646-653.
43. Weiss, M. S., Jabs, A. & Hilgenfeld, R. (1998). Nature Struct. Biol. 5, 676.
44. Winn, M. D. et al. (2011). Acta Cryst. D67, 235-242.