NMR solution structure of human vaccinia-related kinase 1 (VRK1) reveals the C-terminal tail essential for its structural stability and autocatalytic activity

Journal of Biological Chemistry

Volumn 286, Issue 25, 2011, Pages 22131-22138

  Shin, Joon ^a   Chakraborty, Goutam ^a   Bharatham, Nagakumar ^a   Kang, CongBao ^a,d   Tochio, Naoya ^b   Koshiba, Seizo ^b   Kigawa, Takanori ^b   Kim, Wanil ^c   Kim, Kyong Tai ^c   Yoon, Ho Sup ^a  

^a NANYANG TECHNOLOGICAL UNIVERSITY   (Singapore)

^b RIKEN   (Japan)

^c Pohang University of Science and Technology (POSTECH)   (South Korea)

^d Agency for Science   (Singapore)

Author keywords

[No Author keywords available]

Indexed keywords

ATP ANALOGS; AUTOCATALYTIC; C-TERMINAL TAIL; CATALYTIC DOMAINS; CATALYTIC SITES; CELL CYCLE; DELETION MUTANTS; KINASE DOMAINS; NMR STRUCTURES; NMR TITRATION; PROTEIN KINASE; SOLUTION STRUCTURES; STRUCTURAL STABILITIES; TRANSCRIPTION REGULATIONS;

ENZYMES; MAGNETIC DOMAINS; RESONANCE; STABILITY;

NUCLEAR MAGNETIC RESONANCE;

ADENOSINE TRIPHOSPHATE; PROTEIN SERINE THREONINE KINASE; UNCLASSIFIED DRUG; VACCINIA RELATED KINASE 1;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CONTROLLED STUDY; DELETION MUTANT; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STABILITY; ENZYME STRUCTURE; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN MOTIF;

ADENOSINE TRIPHOSPHATE; BIOCATALYSIS; CATALYTIC DOMAIN; ENZYME ACTIVATION; ENZYME STABILITY; HUMANS; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN-SERINE-THREONINE KINASES; SOLUTIONS;

EID: 79959359451     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.200162     Document Type: Article

References (40)

1. Sánchez-Barrena, M. J., Fujii, H., Angulo, I., Martínez-Ripoll, M., Zhu, J. K., and Albert, A. (2007) Mol Cell 26, 427-435
2. Hunter, T. (1995) Cell 80, 225-236
3. Shchemelinin, I., Sefc, L., and Necas, E. (2006) Folia Biol. 52, 81-100
4. Trevino, S. R., Scholtz, J. M., and Pace, C. N. (2007) J. Mol. Biol. 366, 449-460
5. Bossemeyer, D. (1995) FEBS Lett. 369, 57-61
6. Kornev, A. P., and Taylor, S. S. (2010) Biochim. Biophys. Acta 1804, 440-444
7. Hanks, S. K., and Hunter, T. (1995) FASEB J. 9, 576-596
8. Nichols, R. J., and Traktman, P. (2004) J. Biol. Chem. 279, 7934-7946
9. Traktman, P., Anderson, M. K., and Rempel, R. E. (1989) J. Biol. Chem. 264, 21458-21461
10. Sevilla, A., Santos, C. R., Vega, F. M., and Lazo, P. A. (2004) J. Biol. Chem. 279, 27458-27465
11. Klerkx, E. P., Lazo, P. A., and Askjaer, P. (2009) Histol. Histopathol. 24, 749-759
12. Lopez-Borges, S., and Lazo, P. A. (2000) Oncogene 19, 3656-3664
13. Kang, T. H., Park, D. Y., Kim, W., and Kim, K. T. (2008) J. Cell Sci. 121, 3035-3041
14. Nezu, J., Oku, A., Jones, M. H., and Shimane, M. (1997) Genomics 45, 327-331
15. Nichols, R. J., Wiebe, M. S., and Traktman, P. (2006) Mol. Biol. Cell 17, 2451-2464
16. Gorjánácz, M., Klerkx, E. P., Galy, V., Santarella, R., López-Iglesias, C., Askjaer, P., and Mattaj, I. W. (2007) EMBO J. 26, 132-143
17. Segura-Totten, M., Kowalski, A. K., Craigie, R., and Wilson, K. L. (2002) J. Cell Biol. 158, 475-485
18. Segura-Totten, M., and Wilson, K. L. (2004) Trends Cell Biol. 14, 261-266
19. Lancaster, O. M., Cullen, C. F., and Ohkura, H. (2007) J. Cell Biol. 179, 817-824
20. Kang, T. H., Park, D. Y., Choi, Y. H., Kim, K. J., Yoon, H. S., and Kim, K. T. (2007) Mol. Cell. Biol. 27, 8533-8546
21. Nowak, S. J., and Corces, V. G. (2004) Trends Genet. 20, 214-220
22. Scheeff, E. D., Eswaran, J., Bunkoczi, G., Knapp, S., and Manning, G. (2009) Structure 17, 128-138
23. Pervushin, K., Riek, R., Wider, G., and Wüthrich, K. (1997) Proc. Natl. Acad. Sci. U.S.A. 94, 12366-12371
24. Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) J. Biomol. NMR 6, 277-293
25. Goddard, T. D., and Kneller, D. G. (2007) SPARKY, version 3, University of California, San Francisco, CA
26. Ruckert, M., and Otting, G. (2000) J. Am. Chem. Soc. 122, 7793-7797
27. Lukin, J. A., Kontaxis, G., Simplaceanu, V., Yuan, Y., Bax, A., and Ho, C. (2003) Proc. Natl. Acad. Sci. U.S.A. 100, 517-520
28. Valafar, H., and Prestegard, J. H. (2004) J. Mag. Reson. 167, 228-241
29. Güntert, P. (2004) Methods Mol. Biol. 278, 353-378
30. 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., and Warren, G. L. (1998) Acta Crystallogr. D Biol. Crystallogr. 54, 905-921
31. Brunger, A. T. (2007) Nat. Protoc. 2, 2728-2733
32. Shen, Y., Delaglio, F., Cornilescu, G., and Bax, A. (2009) J. Biomol. NMR 44, 213-223
33. Mueller, G. A., Choy, W. Y., Yang, D., Forman-Kay, J. D., Venters, R. A., and Kay, L. E. (2000) J. Mol. Biol. 300, 197-212
34. Koradi, R., Billeter, M., and Wüthrich, K. (1996) J. Mol. Graph. 14, 51-55, 29-32
35. DeLano, W. L. (2002) The PyMOL Molecular Graphics System, version 1.3r1, DeLano Scientific, Palo Alto, CA
36. Barcia, R., López-Borges, S., Vega, F. M., and Lazo, P. A. (2002) Arch. Biochem. Biophys. 399, 1-5
37. Laskowski, R. A., Rullmannn, J. A., MacArthur, M. W., Kaptein, R., and Thornton, J. M. (1996) J. Biomol. NMR 8, 477-486
38. Sessa, F., Mapelli, M., Ciferri, C., Tarricone, C., Areces, L. B., Schneider, T. R., Stukenberg, P. T., and Musacchio, A. (2005) Mol. Cell 18, 379-391
39. Sunami, T., Byrne, N., Diehl, R. E., Funabashi, K., Hall, D. L., Ikuta, M., Patel, S. B., Shipman, J. M., Smith, R. F., Takahashi, I., Zugay-Murphy, J., Iwasawa, Y., Lumb, K. J., Munshi, S. K., and Sharma, S. (2010) J. Biol. Chem. 285, 4587-4594
40. Chen, L., Jiao, Z. H., Zheng, L. S., Zhang, Y. Y., Xie, S. T., Wang, Z. X., and Wu, J. W. (2009) Nature 459, 1146-1149