The spectrin repeat folds into a three-helix bundle in solution

FEBS Letters

Volumn 383, Issue 3, 1996, Pages 201-207

  Pascual, Jaime ^a   Pfuhl, Mark ^a   Rivas, German ^b   Pastore, Annalisa ^a   Saraste, Matti ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^b CENTRO DE INVESTIGACIONES BIOLÓGICAS   (Spain)

Author keywords

Heteronuclear NMR; Membrane skeleton; Spectrin repeat; Three helix bundle

Indexed keywords

SPECTRIN;

ANIMAL TISSUE; ARTICLE; BRAIN; CHICKEN; CONTROLLED STUDY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE;

ANIMALIA; GALLUS GALLUS;

EID: 0029863942     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/0014-5793(96)00251-7     Document Type: Article

References (53)

1. Elgsaeter, A., Stokke, B.T., Mikkelsen, A. and Branton, D. (1986) Science 234, 1217-1222.
2. Bennett, V. and Gilligan, D.M. (1993) Annu. Rev. Cell Biol. 9, 27-66.
3. Sheterline, P., Clayton, J. and Sparrow, J. (1995) Protein Profile 2, 1-68.
4. Hartwig, J.H. (1994) Protein Profile 1, 711-762.
5. Castresana, J. and Saraste, M. (1995) FEBS Lett. 374, 149-151.
6. Trave, G., Pastore, A., Hyvonen, M. and Saraste, M. (1995) Eur. J. Biochem. 227, 35-42.
7. Trave, G., Lacombe, P.J., Pfuhl, M., Saraste, M. and Pastore, A. (1995) EMBO J. 14, 4922-4931.
8. Viel, A. and Branton, D. (1994) Proc. Natl. Acad. Sci. USA 91, 10839-10843.
9. Tse, W.T., Lecomte, M.C., Costa, F.F., Garbarz, M., Feo, C., Boivin, P., Dhermy, D. and Forget, B.G. (1990) J. Clin. Invest. 86, 909-916.
10. Musacchio, A., Noble, M., Pauptit, R., Wirenga, R. and Saraste, M. (1992) Nature 359, 851-854.
11. Macias, M.J., Musacchio, A., Ponstingl, H., Nilges, M., Saraste, M. and Oschkinat, H. (1994) Nature 369, 675-677.
12. Speicher, D.W. and Marchesi, V.T. (1984) Nature 311, 177-180.
13. Winograd, E., Hume, D. and Branton, D. (1991) Proc. Natl. Acad. Sci. USA 88, 10788-10791.
14. Lusitani, D.M., Qtaishat, N., LaBrake, C.C., Yu, R.N., Davis, J., Kelley, M.R. and Fung, L.W. (1994) J. Biol. Chem. 269, 25955-25958.
15. MacDonald, R.I., Musacchio, A., Holmgren, R.A. and Saraste, M. (1994) Proc. Natl. Acad. Sci. USA 91, 1299-1303.
16. Parry, D.A., Dixon, T.W. and Cohen, C. (1992) Biophys. J. 61, 858-867.
17. Lupas, A., Van Dyke, M. and Stock, J. (1991) Science 252, 1162-1164.
18. Yan, Y., Winograd, E., Viel, A., Cronin, T., Harrison, S.C. and Branton, D. (1993) Science 262, 2027-2030.
19. Wasenius, V.M., Saraste, M., Salven, P., Eramaa, M., Holm, L. and Lehto, V.P. (1989) J. Cell. Biol. 108, 79-93.
20. Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A. and Struhl, K. (1992) Current Protocols in Molecular Biology, Wiley, New York.
21. Studier, F.W., Rosenberg, A.H., Dunn, J.J. and Dubendorff, J.W. (1990) Methods Enzymol. 185, 60-89.
22. Laemmli, U. (1970) Nature 227, 680-685.
23. Gill, S.C. and Hippel, P.H. (1989) Anal. Biochem. 182, 319-326.
24. Sambrook, J., Fritsch, E.F. and Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory Press, Plainview, NY.
25. Ralston, G. (1993) Introduction to Analytical Ultracentrifugation, Beckman Instruments Inc., Palo Alto, CA.
26. Minton, A.P. (1994) Modern Analytical Ultracentrifugation, pp. 81-93, Birkhauser, Boston.
27. Laue, T.M., Shah, B.D., Ridgeway, T.M. and Pelletier, S.L. (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science, pp. 90-125, Royal Society of Chemistry, Cambridge.
28. Piotto, M., Saudek, V. and Sklenar, V. (1992) J. Biomol. NMR 2, 661-665.
29. Sklenar, V., Piotto, M., Leppik, R. and Saudek, V. (1993) J. Magn. Reson. A 102, 241-245.
30. Stonehouse, J., Shaw, G.L., Keeler, J. and Laue, E.D. (1994) J. Magn. Reson. A 107, 178-184.
31. Kay, L.E. and Bax, A. (1990) J. Magn. Reson. 86, 110-126.
32. Barbato, G., Ikura, M., Kay, L.E., Pastor, R.W. and Bax, A. (1992) Biochemistry 31, 5269-5278.
33. Kay, L.E., Torchia, D.A. and Bax, A. (1989) Biochemistry 28, 8972-8979.
34. Kay, L.E., Nicholson, L.K., Delagio, F., Bax, A. and Torchia, D.A. (1992) J. Magn. Reson. 97, 359-367.
35. Kadkhodaei, M., Hwang, T.L., Tang, J. and Shaka, A.J. (1993) J. Magn. Reson. A 104, 105-107.
36. Majumdar, A. and Zuiderweg, E.P. (1993) J. Magn. Reson. B 102, 242-244.
37. Kay, L.E., Ikura, M., Tschudin, R. and Bax, A. (1990) J. Magn. Reson. 89, 496-514.
38. Grzesiek, S. and Bax, A. (1992) J. Magn. Reson. 96, 432-440.
39. Clubb, R.T., Thanabal, V. and Wagner, G. (1992) J. Magn. Reson. 97, 213-217.
40. Marion, D., Ikura, M., Tschudin, R. and Bax, A. (1989) J. Magn. Reson. 85, 393-397.
41. Boucher, W. (1994) AZARA v1.0, Department of Biochemistry, University of Cambridge, UK.
42. Wishart, D.S., Bigam, C.G., Yao, J., Abildgaard, F., Dyson, J., Oldfield, E., Markley, J. and Sykes, B.D. (1995) J. Biomol. NMR 6, 135-140.
43. Wüthrich, K., Billeter, M. and Braun, W. (1984) J. Mol. Biol. 180, 715-740.
44. Wüthrich, K. (1986) NMR of Proteins and Nucleic Acids, Wiley, New York.
45. Pastore, A. and Saudek, V. (1990) J. Magn. Reson. 90, 165-176.
46. Wishart, D.S., Sykes, B.D. and Richards, F.M. (1992) Biochemistry 31, 1647-1651.
47. Wishart, D.S. and Sykes, B.D. (1994) J. Biomol. NMR 4, 171-180.
48. Lipari, G. and Szabo, A. (1982) J. Am. Chem. Soc. 104, 4546-4559.
49. Lipari, G. and Szabo, A. (1982) J. Am. Chem. Soc. 104, 4559-4570.
50. Clore, G.M., Szabo, A., Bax, A., Kay, L.E., Driscoll, P.C. and Gronenborn, A.M. (1990) J. Am. Chem. Soc. 112, 4989-4991.
51. Redfield, C., Boyd, J., Smith, L.J., Smith, R.A.G. and Dobson, C.M. (1992) Biochemistry 31, 10431-10437.
52. Mandel, A.M., Akke, M. and Palmer III, A.G. (1995) J. Mol. Biol. 246, 144-163.
53. Kabsch, W. and Sander, C. (1983) Biopolymers 22, 2577-2637.