Structural insights into the mechanism of calmodulin binding to death receptors

Acta Crystallographica Section D: Biological Crystallography

Volumn 70, Issue 6, 2014, Pages 1604-1613

  Cao, Peng ^a   Zhang, Wenting ^a,c   Gui, Wenjun ^a   Dong, Yuhui ^b   Jiang, Tao ^a   Gong, Yong ^b  

^a INSTITUTE OF BIOPHYSICS   (China)

^b INSTITUTE OF HIGH ENERGY PHYSICS   (China)

^c UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

Author keywords

calmodulin; death domain; death receptor; DR6; Fas

Indexed keywords

CALMODULIN; DEATH RECEPTOR;

AMINO ACID SEQUENCE; ANIMAL; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; METABOLISM; MOLECULAR GENETICS; PC12 CELL LINE; PROTEIN CONFORMATION; RAT; SEQUENCE HOMOLOGY; SURFACE PLASMON RESONANCE; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CALMODULIN; CRYSTALLOGRAPHY, X-RAY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PC12 CELLS; PROTEIN CONFORMATION; RATS; RECEPTORS, DEATH DOMAIN; SEQUENCE HOMOLOGY, AMINO ACID; SURFACE PLASMON RESONANCE;

EID: 84902441493     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S1399004714006919     Document Type: Article

References (45)

1. Ahn, E.-Y., Lim, S.-T., Cook, W. J. & McDonald, J. M. (2004). J. Biol. Chem. 279, 5661-5666.
2. Benschop, R.,Wei, T. & Na, S. (2009). Therapeutic Targets of the TNF Superfamily, edited by I. S. Grewal, pp. 186-194. New York: Springer.
3. 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.
4. Chen, Y., Pawar, P., Pan, G., Ma, L., Liu, H. & McDonald, J. M. (2008). J. Cell. Biochem. 103, 788-799.
5. Egea, J., Espinet, C., Soler, R. M., Dolcet, X., Yuste, V. J., Encinas,M., Iglesias,M., Rocamora, N. & Comella, J. X. (2001). J. Cell Biol. 154, 585-597.
6. Egea, J., Espinet, C., Soler, R. M., Peiró, S., Rocamora, N. & Comella, J. X. (2000). Mol. Cell. Biol. 20, 1931-1946.
7. Emsley, P. & Cowtan, K. (2004). Acta Cryst. D60, 2126-2132.
8. Ferrao, R. & Wu, H. (2012). Curr. Opin. Struct. Biol. 22, 241-247.
9. Gong, Y., Cao, P., Yu, H.-J. & Jiang, T. (2008). Nature (London), 454, 789-793.
10. Gouet, P., Courcelle, E., Stuart, D. I. & Métoz, F. (1999). Bioinformatics, 15, 305-308.
11. Hoeflich, K. P. & Ikura, M. (2002). Cell, 108, 739-742.
12. Hong, K., Nishiyama, M., Henley, J., Tessier-Lavigne, M. & Poo, M. (2000). Nature (London), 403, 93-98.
13. Horváth, I., Harmat, V., Perczel, A., Pálfi, V., Nyitray, L., Nagy, A., Hlavanda, E., Náray-Szabó, G. & Ovádi, J. (2005). J. Biol. Chem. 280, 8266-8274.
14. Huang, B., Eberstadt, M., Olejniczak, E. T., Meadows, R. P. & Fesik, S. W. (1996). Nature (London), 384, 638-641.
15. Ibáñ ez, C. F. & Simi, A. (2012). Trends Neurosci. 35, 431-440.
16. Kincaid, R. L., Billingsley, M. L. & Vaughan, M. (1988). Methods Enzymol. 159, 605-626.
17. Kong, H., Kim, A. H., Orlinick, J. R. & Chao, M. V. (1999). Cell Death Differ. 6, 1133-1142.
18. Laskowski, R. A., MacArthur, M. W., Moss, D. S. & Thornton, J. M. (1993). J. Appl. Cryst. 26, 283-291.
19. Lavrik, I., Golks, A. & Krammer, P. H. (2005). J. Cell Sci. 118, 265-267.
20. Li, Y., Jia, Y.-C., Cui, K., Li, N., Zheng, Z.-Y., Wang, Y.-Z. & Yuan, X.-B. (2005). Nature (London), 434, 894-898.
21. Liepinsh, E., Ilag, L. L., Otting, G. & Ibáñ ez, C. F. (1997). EMBO J. 16, 4999-5005.
22. Matsubara, M., Nakatsu, T., Kato, H. & Taniguchi, H. (2004). EMBO J. 23, 712-718.
23. Maximciuc, A. A., Putkey, J. A., Shamoo, Y. & Mackenzie, K. R. (2006). Structure, 14, 1547-1556.
24. Mc Guire, C., Beyaert, R. & van Loo, G. (2011). Trends Neurosci. 34, 619-628.
25. Meador, W. E., Means, A. R. & Quiocho, F. A. (1992). Science, 257, 1251-1255.
26. Meador, W. E., Means, A. R. & Quiocho, F. A. (1993). Science, 262, 1718-1721.
27. 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.
28. Nykjaer, A., Willnow, T. E. & Petersen, C. M. (2005). Curr. Opin. Neurobiol. 15, 49-57.
29. O' Reilly, L. A., Tai, L., Lee, L., Kruse, E. A., Grabow, S., Fairlie, W. D., Haynes, N. M., Tarlinton, D. M., Zhang, J. G., Belz, G. T., Smyth, M. J., Bouillet, P., Robb, L. & Strasser, A. (2009). Nature (London), 461, 659-663.
30. Osawa, M., Tokumitsu, H., Swindells, M. B., Kurihara, H., Orita, M., Shibanuma, T., Furuya, T. & Ikura, M. (1999). Nature Struct. Biol. 6, 819-824.
31. Otwinowski, Z. & Minor, W. (1997). Methods Enzymol. 276, 307-326.
32. Pan, D., Yan, Q., Chen, Y., McDonald, J. M. & Song, Y. (2011). Proteins, 79, 2543-2556.
33. Park, H. H., Lo, Y.-C., Lin, S.-C., Wang, L., Yang, J. K. & Wu, H. (2007). Annu. Rev. Immunol. 25, 561-586.
34. Rabizadeh, S. et al. (2000). J. Mol. Neurosci. 15, 215-229.
35. Salvesen, G. S. & Riedl, S. J. (2009). Cell Cycle, 8, 2723-2727.
36. Scott, F. L., Stec, B., Pop, C., Dobaczewska, M. K., Lee, J. J., Monosov, E., Robinson, H., Salvesen, G. S., Schwarzenbacher, R. & Riedl, S. J. (2009). Nature (London), 457, 1019-1022.
37. Vagin, A. & Teplyakov, A. (2010). Acta Cryst. D66, 22-25.
38. Vandonselaar, M., Hickie, R. A., Quail, J. W. & Delbaere, L. T. J. (1994). Nature Struct. Biol. 1, 795-801.
39. Vetter, S. W. & Leclerc, E. (2003). Eur. J. Biochem. 270, 404-414.
40. Wallace, A. C., Laskowski, R. A. & Thornton, J. M. (1995). Protein Eng. 8, 127-134.
41. Wang, L., Yang, J. K., Kabaleeswaran, V., Rice, A. J., Cruz, A. C., Park, A. Y., Yin, Q., Damko, E., Jang, S. B., Raunser, S., Robinson, C. V., Siegel, R. M., Walz, T. & Wu, H. (2010). Nature Struct. Mol. Biol. 17, 1324-1329.
42. Wilson, N. S., Dixit, V. & Ashkenazi, A. (2009). Nature Immunol. 10, 348-355.
43. Winn, M. D. et al. (2011). Acta Cryst. D67, 235-242.
44. Wu, X., Ahn, E. Y., McKenna, M. A., Yeo, H. & McDonald, J. M. (2005). J. Biol. Chem. 280, 29964-29970.
45. Yamashita, T. & Tohyama, M. (2003). Nature Neurosci. 6, 461-467.