Solution structure of nodularin: An inhibitor of serine/threonine- specific protein phosphatases

Journal of Biological Chemistry

Volumn 271, Issue 28, 1996, Pages 16695-16702

  Annila, Arto ^a   Lehtimäki, Jaana ^b   Mattila, Kimmo ^c   Eriksson, John E ^d   Sivonen, Kaarina ^b   Rantala, Tapio T ^c   Drakenberg, Torbjörn ^a  

^a VTT TECHNICAL RESEARCH CENTRE OF FINLAND   (Finland)

^b UNIVERSITY OF HELSINKI   (Finland)

^c UNIVERSITY OF OULU   (Finland)

^d TURKU CENTRE FOR BIOTECHNOLOGY   (Finland)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID DERIVATIVE; ARGININE; ASPARTIC ACID DERIVATIVE; CYANOGINOSIN LR; NODULARIN; PHOSPHOPROTEIN PHOSPHATASE INHIBITOR; SERINE; SOLVENT; THREONINE; WATER;

ARTICLE; CALCULATION; HYDROGEN BOND; MOLECULAR DYNAMICS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN STRUCTURE; STEREOCHEMISTRY;

ENZYME INHIBITORS; MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDES, CYCLIC; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN CONFORMATION;

EID: 0029941728     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.271.28.16695     Document Type: Article

References (60)

1. Cohen, P. (1989) Annu. Rev. Biochem. 58, 453-508
2. MacKintosh, C., and MacKintosh, R. W. (1994) Trends Biochem. Sci. 19, 444-448
3. Bialojan, C., and Takai, A. (1988) Biochem. J. 266, 283-290
4. MacKintosh, C., Beatlie, K. A., Klumpp, S., Cohen, P., and Codd, G. A. (1990) FEBS Lett. 264, 187-192
5. Honkanen, R. E., Zwiller, J., Moore, R. E., Daly, S. L., Khatra, B., Dukelow, M., and Boynton, A. L. (1990) J. Biol. Chem. 265, 19401-19404
6. Eriksson, J. E., Brautigan, D. L., Vallee, R., Olmsted, J., Fujiki, H., and Goldman, R. D. (1992) Proc. Natl. Acad. Sci. U. S. A. 89, 11093-11097
7. Eriksson, J. E., and Goldman, R. D. (1993) Adv. Protein Phosphatases 7, 335-357
8. Mellgren, G., Vintermyr, O. K., Bøe, R., and Døskeland, S. O. (1993) Exp. Cell Res. 205, 293-301
9. Ishida, Y., Furukawa, Y., Decaprio, J. A., Saito, M., and Griffin, J. D. (1992) J. Cell. Physiol. 150, 484-492
10. Eriksson, J. E., Grönberg, L., Nygård, S., Slotte, J. P., and Meriluoto, J. A. O. (1990) Biochim. Biophys. Acta 1025, 60-66
11. Meriluoto, J. A. O., Nygård, S. E., Dahlem, A. M., and Eriksson, J. E. (1990) Toxicon 28, 1439-1446
12. Eriksson, J. E., Toivola, D., Meriluoto, J. A. O., Karaki, H., Han, Y.-G., and Hartshorne, D. (1990) Biochem. Biophys. Res. Commun. 173, 1347-1353
13. Eriksson, J. E., and Goldman, R. D. (1993) Adv. Protein Phosphatases 7, 335-357
14. Deleted in proof
15. Nishiwaki-Matsushima, R., Ohta, T., Nishiwaki, S., Suganuma, M., Kohyama, K., Ishikawa, T., Carmichael, W. W., and Fujiki, H. (1992) J. Cancer Res. Clin. Oncol. 118, 420-424
16. Carmichael, W. W. (1988) Hondb. Nat. Toxins 3, 121-147
17. Carmichael, W. W., Beasley, V. R., Bunner, D. L., Eloff, J. N., Falconer, I., Gorham, P., Harada, K.-I., Krishnamurthy, T., Yu, M. J., Moore, R. E., Rihehart, K. L., Runnegar, M., Skulberg, O. M., and Watanabe, M. (1988) Toxicon 26, 971-973
18. Rinehart, K. L., Harada, K.-I., Namikoshi, M., Chen, C., Harvey, C. A., Munro, M. H. G., Blunt, J. W., Mulligan, P. E., Beasley, V. R., Dahlem, A. M., and Carmichael, W. W. (1988) J. Am. Chem. Soc. 110, 8557-8558
19. Carmichael, W. W., Eschedor, J. T., Patterson, G. M. L., and Moore, R. E. (1988) Appl Environ. Microbiol. 54, 2257-2263
20. Eriksson, J. E., Meriluoto, J. A. O., Kujari, H. P., Österlund, K., Fagerlund, K., and Hällbom, L. (1988) Toxicon 26, 161-166
21. Sivonen, K., Kommen, K., Esala, A.-L., and Niemelä, S. I. (1989) Hydrobiologia 185, 3-8
22. Matsushima, R., Yoshizawa, S., Watanabe, M. F., Harada, K., Furusawa, M., Carmichael, W. W., and Fujiki, H. (1990) Biochem. Biophys. Res. Commun. 171, 867-874
23. Moorhead, G., MacKintosh, R. W., Morrice, N., Gallagher, T., and MacKintosh, C. (1994) FEBS Lett. 366, 46-50
24. Halkides, C. J., and Redfield, A. G. (1995) J. Biomol. NMR 5, 362-366
25. Rudolpf-Böhner, S., Mierke, D. F., and Moroder, L. (1994) FEBS Lett. 349, 319-323
26. Trogen, G.-B., Annila, A., Eriksson, J. E., Kontteli, M., Meriluoto, J., Setson, I., Zdunek, J., and Edlund, U. (1996) Biochemistry 35, 3197-3205
27. Bagu, J. R., Sönnichsen, F. D., Williams, D., Andersen, R. J., Sykes, B. D., and Holmes, C. F. B. (1995) Struct. Biol. 2, 114-116
28. DeSilva, S. D., Williams, D. E., Andersen, R. J., Klix, H., Holmes, C. F. B., and Allen, T. M. (1992) Tetrahedron Lett. 33, 1561-1564
29. Barford, D., and Keller, J. C. (1994) J. Mol. Biol. 235, 763-766
30. Egloff, M.-P., Cohen, P. T. W., Reinemer, P., and Barford, D. (1995) J. Mol. Biol. 254, 942-959
31. Goldberg, J., Huang, H.-B., Kwon, Y.-G., Greengard, P., Nairn, A., and Kuriyan, J. (1995) Nature 376, 745-753
32. Zhang, Z., Bai, G., Deans-Zirattu, S., Browner, M. F., and Lee, E. Y. C. (1992) J. Biol. Chem. 267, 1484-1490
33. MacKintosh, R. W., Dalby, K. N., Campbell, D. G., Cohen, P. T. W., Cohen, P., and MacKintosh, C. (1995) FEBS Lett. 371, 236-240
34. Rouhiainen, L., Sivonen, K., Buikema, W., and Haselkorn, R. (1995) J. Bacteriol. 177, 6021-6026
35. Sivonen, K., Kononen, K., Carmichael, W. W., Dahlem, A. M., Rinehart, K., Kiviranta, J., and Niemelä, S. I. (1989) Appl. Environ. Microbiol. 55, 1990-1995
36. Lehtimäki, J., Sivonen K., Luukkainen, R., and Niemelä, S. I. (1994) Arch. Hydrobiol. 130, 269-282
37. Martin, M. L., Delpuech, J.-J., and Martin, G. L. (1980) Practical NMR Spec- troscopy, Heyden, London
38. States, D. J., Haberkorn, R., and Ruben, D. (1982) J. Magn. Reson. 55, 151
39. Marion, D., Ikura, M., Tschudin, R., and Bax A. (1989) J. Magn. Reson. 85, 393-399
40. Cavanagh, J., and Rance, M. (1990) J. Magn. Reson. 88, 72-85
41. Shaka, A. J., Lee, C. J., and Pines, A. (1988) J. Magn. Reson. 77, 274-293
42. Sodano, P., and Delepierre, M. (1993) J. Magn. Reson. 104, 88-92
43. Namikoshi, M., Choi, B. W., Sakai, R., Sun, F., and Rinehart, K. L. (1994) J. Org. Chem. 59, 2349-2357
44. Harada, K.-I., Ogawa, K., Matsuura, K., Murata, H., Suzuki, M., Watanabe, M. F., Itzeno, Y., and Nakayama, N. (1990) Chem. Res. Toxicol. 3, 473-481
45. Bundi, A., and Wüthrich, K. (1979) Biopolymers 18, 285-298
46. McIntyre, L., and Freeman, R. (1992) J. Magn. Reson. 96, 425-431
47. Bystrow, V. F. (1976) Prog. Nucl. Magn. Reson. Spectrosc. 10, 41-81
48. Havel, T. F., Crippen, G. M., and Kuntz, I. D. (1979) Biopolymers 18, 73
49. Biosym Technologies (1994) NMRchitecht User Guide 5, Version 2.3, Biosym Technologies, San Diego, CA
50. Boelens, R., Koning, T. M. G., and Kaptain, R. (1988) J. Mol. Struct. 173, 299-311
51. Molecular Simulations Inc. (1994) Quanta, Molecular Simulations Inc., Burlington, MA
52. Biosym Technologies (1993) DMol User Guide 5, Version 2.3, Biosym Technologies, San Diego, CA
53. Rantala, T. T., Wästberg, B., and Rosén, A. (1986) Chem. Phys. 109, 261-268
54. Vosko, S. J., Wilk, L., and Nusair, M. (1980) Can. J. Phys. 58, 1200-1211
55. Hirschfeld, F. L. (1977) Theor. Chim. Acta (Berl.) 44, 129-138
56. Brooks, B. R., Bruccoleri, R. E., Olafson, B. D., States, D. J., Swaminathan, S., and Karplus, M. (1983) J. Comp. Chem. 4, 187-217
57. Molecular Simulations Inc. (1992) CHARMm, Molecular Simulations Inc., Burlington, MA
58. van Gunsteren, W. F., and Berendsen, H. J. C. (1977) Mol. Physiol. 34, 1311-1327
59. Jorgensen, W. L. (1982) J. Chem. Phys. 77, 4156-4163
60. Laaksonen, L. (1992) J. Mol. Graph. 10, 33