Effects of glycosylation on the structure and dynamics of eel calcitonin in micelles and lipid bilayers determined by nuclear magnetic resonance spectroscopy

Biochemistry

Volumn 38, Issue 26, 1999, Pages 8377-8384

  Hashimoto, Yasuhiro ^a   Toma, Kazunori ^b   Nishikido, Joji ^b   Yamamoto, Keizo ^b   Haneda, Katsuji ^b   Inazu, Toshiyuki ^b   Valentine, Kathleen G ^b   Opella, Stanley J ^b  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

CALCITONIN;

ALPHA HELIX; ARTICLE; CARBOXY TERMINAL SEQUENCE; CHEMICAL STRUCTURE; EEL; GLYCOSYLATION; LIPID BILAYER; MICELLE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; STRUCTURE ANALYSIS;

ACETYLGLUCOSAMINE; AMINO ACID SEQUENCE; ANIMALS; CALCITONIN; CARBOHYDRATE CONFORMATION; CARBOHYDRATE SEQUENCE; CRYSTALLOGRAPHY, X-RAY; EELS; GLYCOSYLATION; LIPID BILAYERS; MICELLES; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY; STRUCTURE-ACTIVITY RELATIONSHIP; THERMODYNAMICS;

ANGUILLIFORMES; VERTEBRATA;

EID: 0033614823     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi983018j     Document Type: Article

References (41)

1. Recny, M. A., Luther, M. A., Knoppers, M. H., Neidhardt, E. A., Khandekar, S. S., Concino, M. F., Schimke, P. A., Francis, M. A., Moebius, U., Reinhold, B. B., Reinhold, V. N., and Reinherz, E. L. (1992) J. Biol. Chem. 267, 22428-22434.
2. Rudd, P. M., Joao, H. C., Coghill, E., Fiten, P., Saunders, M. R., Opdenakker, G., and Dwek, R. A. (1994) Biochemistry 33, 17-22.
3. Kessler, H., Matter, H., Gemmecker, G., Kottenhahn, M., and Bats, J. W. (1992) J. Am. Chem. Soc. 114, 4805-4818.
4. Shogren, R., Gerken, T. A., and Jentoft, N. (1989) Biochemistry 28, 5525-5536.
5. Gerken, T. A., Butenhof, K. J., and Shogren, R. (1989) Biochemistry 28, 5536-5543.
6. Shaanan, B., Lis, H., and Sharon, N. (1991 ) Science 254, 862-866.
7. Joao, H. C., Scragg, I. G., and Dwek, R. A. (1992) FEBS Lett. 307, 343-346.
8. Andreotti, A. H., and Kahne, D. (1993) J. Am. Chem. Soc. 115, 3352-3353.
9. Imperiali, B., and Rickert, K. W. (1995) Proc. Natl. Acad. Sci. U.S.A. 92, 97-101.
10. Inazu, T., and Kobayashi, K. (1993) Synlett 869-870.
11. Inazu, T., Mizuno, M., Kohda, Y., Kobayashi, K., and Yaginuma, H. (1996) in Peptide Chemistry 1995 (Nishi, N., Ed.) pp 61-64, Protein Research Foundation, Osaka, Japan.
12. Haneda, K., Inazu, T., Yamamoto, K., Kumagai, H., Nakahara, Y., and Kobata, A. (1996) Carbohydr. Res. 292, 61-70.
13. Mizuno, M., Muramoto, I., Kawakami, T., Seike, M., Aimoto, S., Haneda, K., and Inazu, T. (1998) Tetrahedron Lett. 39, 55-58.
14. Haneda, K., Inazu, T., Mizuno, M., Iguchi, R., Yamamoto, K., Kumagai, H., Aimoto, S., Suzuki, H., and Noda, T. (1998) Bioorg. Med. Chem. Lett. 8, 1303-1306.
15. Yamamoto, K., Haneda, K., Iguchi, R., Inazu, T., Mizuno, M., Takegawa, K., Kondo, A., and Kato, I. (1999) J. Biosci. Bioeng. 87, 175-179.
16. Mizuno, M., Haneda, K., Iguchi, R., Muramoto, I., Kawakami, T., Aimoto, S., Yamamoto, K., and Inazu, T. (1999) J. Am. Chem. Soc. 121, 284-290.
17. Motta, A., Antonietta, M., Morelli, C., Goud, N., and Temussi, P. A. (1989) Biochemistry 28, 7996-8002.
18. Meadows, R. P., Nikonowicz, E. P., Jones, C. R., Bastian, J. W., and Gorenstein, D. G. (1991) Biochemistry 30, 1247-1254.
19. Motta, A., Temussi, P. A., Wünsch, E., and Bovermann, G. (1991) Biochemistry 30, 2364-2371.
20. Motta, A., Pastore, A., Goud, N. A., and Morelli, M. A. C. (1991) Biochemistry 30, 10444-10450.
21. Ogawa, K., Nishimura, S., Doi, M., Kyogoku, Y., Hayashi, M., and Kobayashi, Y. (1994) Eur. J. Biochem. 222, 659-666.
22. Motta, A., Andreotti, G., Amondeo, P., Strazzullo, G., and Morelli, M. A. C. (1998) Proteins 32, 314-323.
23. Epand, R. M., Epand, R. F., Orlowski, R. C., Schlueter, R. J., Boni, L. T., and Hui, S. W. (1983) Biochemistry 22, 5074-5084.
24. Epand, R. M., and Epand, R. F. (1986) Biochemistry 25, 1964-1968.
25. Murad, F., Brewer, H. B., and Vaughan, M. (1970) Proc. Natl. Acad. Sci. U.S.A. 65, 446-453.
26. Lin, H. Y., Harris, T. L., Flannery, M. S., Aruffo, A., Kaji, E. H., Gorn, A., Kolakowski, L. F., Lodish, H. F., and Goldring, S. R. (1991) Science 254, 1022-1026.
27. Opella, S. J. (1997) Nature Struct. Biol., NMR Suppl. 4, 845-848.
28. Cross, T. A., and Opella, S. J. (1994) Curr. Opin. Struct. Biol. 4, 574-581.
29. Marassi, F. M., and Opella, S. J (1998) Curr. Opin. Struct. Biol. 8, 640-648.
30. Marassi, F. M., Ramamoorthy, A., and Opella, S. J. (1997) Proc. Natl. Acad. Sci. U.S.A. 94, 8551-8556.
31. Kim, Y., Valentine, K., Opella, S. J., Schendel, S. L., and Cramer, W. A. (1998) Protein Sci. 7, 342-348.
32. Opella, S. J., Marassi, F. M., Gesell, J., Valente, A. P., Kim, Y., Oblatt-Montal, M., and Montal, M. (1999) Nature Struct. Biol. 6, 374-379.
33. Wu, C. H., Ramamoorthy, A., and Opella, S. J. (1994) J. Magn. Reson., Ser. A 109, 270-272.
34. Wüthrich, K. (1986) NMR of Proteins and Nucleic Acids, J. Wiley & Sons, New York.
35. Harbison, G. S., Jelinski, L. W., Stark, R. E., Torchia, D. A., Herzfeld, J., and Griffin, R. G. (1984) J. Magn. Reson. 60, 79-82.
36. Oas, T. G., Hartzell, C. J., Dahlquist, F. W., and Drobny, G. P. (1987) J. Am.Chem. Soc. 109, 5962-5966.
37. Hartzell, C. J., Whitfield, M., Oas, T. G., and Drobny, G. P. (1987) J. Am. Chem. Soc. 109, 5966-5969.
38. Teng, Q., and Cross, T. A. (1989) J. Magn. Reson. 85, 439-447.
39. Mer, G., Hietter, H., and Lefèvre, J. F. (1996) Nature Struct. Biol. 3, 45-53.
40. Wyss, D. F., Choi, J. S., Li., J., Knoppers, M. H., Willis, K. J., Arulanandam, A. R. N., Smolyar, A., Reinhertz, E. L., and Wagner, G. (1995) Science 269, 1273-1277.
41. O'Neil, J. D. J., and Sykes, B. D. (1989) Biochemistry 28, 699-707.