Leucine is the most stabilizing aliphatic amino acid in the d position of a dimeric leucine zipper coiled coil

Biochemistry

Volumn 36, Issue 41, 1997, Pages 12567-12573

  Moitra, Jaideep ^a   Szilák, Lászlo ^a   Krylov, Dmitry ^a   Vinson, Charles ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ALIPHATIC COMPOUND; AMINO ACID; DIMER; ISOLEUCINE; LEUCINE; LEUCINE ZIPPER PROTEIN; VALINE;

AMINO ACID SUBSTITUTION; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; PRIORITY JOURNAL; PROTEIN STABILITY; THERMOSTABILITY;

AMINO ACID SEQUENCE; DIMERIZATION; DNA-BINDING PROTEINS; LEUCINE ZIPPERS; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN DENATURATION; TEMPERATURE;

EID: 0030804094     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi971424h     Document Type: Article

References (43)

1. Alber, T. (1992) Curr. Opin. Genet. Dev. 2, 205-210.
2. Baxevanis, A., & Vinson, C. (1993) Curr. Opin. Genet. Dev. 3, 278-285.
3. Cohen, C., & Parry, D. (1990) Protein 7, 1-14.
4. Creamer, T., & Rose, G. (1995) Protein Sci. 4, 1305-1314.
5. Crick, F. (1953) Acta Crystallogr. 6, 689-697.
6. Ellenberger, T., Brandi, C., Struhl, K., & Harrison, S. (1992) Cell 71, 1223-1237.
7. Eriksson, A., Baase, W., Zhang, X., Heinz, D., Blaber, M., Baldwin, E., & Matthews, B. (1992) Science 255, 178-183.
8. Fauchere, J., & Pliska, V. (1983) Eur. J. Med. Chem. 18, 369-375.
9. Fonjallaz, P., Ossipow, V., Wanner, G., & Schibler, U. (1996) EMBO J. 15, 351-362.
10. Glover, M., & Harrison, S. (1995) Nature 373, 257-261.
11. Harbury, P. B., Zhang, T., Kim, P., & Abler, T. (1993) Science 262, 1401-1407.
12. Harbury, P. B., Kim, P. S., & Alber, T. (1994) Nature 371, 80-83.
13. Ho, S., Hunt, H., Horton, R., Pullen, J., & Pease, L. (1989) Gene 77, 51-59.
14. Hu, J., O'Shea, E., Kim, P., & Sauer, R. (1990) Science 250, 1400-1403.
15. Hurst, H. (1995) Protein Profile 2, 105-168.
16. Iyer, S., Davis, D., Seal, S., & Burch, J. (1991) Mol. Cell. Biol. 11, 4863-4875.
17. Kouzarides, T., & Ziff, E. (1988) Nature 336, 646-651.
18. Krylov, D., Mikhailenko, I., & Vinson, C. (1994) EMBO J. 13, 1849-1861.
19. Krylov, D., Olive, M., & Vinson, C. (1995) EMBO J. 14, 5329-5337.
20. Laemmli, U. (1970) Nature 277, 680-685.
21. Landschultz, W., Johnson, P., & McKnight, S. (1988) Science 240, 1759-1764.
22. Landschultz, W., Johnson, P., & McKnight, S. (1989) Science 243, 1681-1688.
23. Lee, B., & Vasmatzis, G. (1997) Curr. Opin. Biotechnol. 8, 423-428.
24. Lupas, A. (1996) Trends Biochem. Sci. 21, 375-382.
25. Olive, M., Krylov, D., Echlin, D., Gardner, G., Taparowsky, B. J., & Vinson, C. (1997) J. Biol. Chem. 272, 18586-18594.
26. O'Neil, K., & DeGrado, W. (1990) Science 250, 646-651.
27. O'Shea, E., Klemm, J., Kim, P., & Abler, T. (1991) Science 254, 539-544.
28. Pace, C. (1995) Methods Enzymol. 259, 538-554.
29. Pace, C., Shirley, B., Mcnutt, M., & Gajiwala, K. (1996) FASEB J. 10, 75-83.
30. Padmanabhan, S., & Baldwin, R. (1994) Protein Sci. 3, 1992-1997.
31. Ponder, J., & Richards, F. (1987) J. Mol. Biol. 193, 775-791.
32. Sanger, F., Nicklen, S., & Coulson, A. (1977) Proc. Natl. Acad. Sci. U.S.A. 74, 5463-5467.
33. Serrano, L., Kellis, J., Cann, P., Matouschek, A., & Fersht, A. (1992) J. Mol. Biol. 224, 783-804.
34. Shortle, D., Stites, W., & Meeker, A. (1990) Biochemistry 29, 8033-8041.
35. Studier, F. W., & Moffatt, B. A. (1986) J. Mol. Biol. 189, 113-130.
36. Thompson, K., Vinson, C., & Freire, E. (1993) Biochemistry 32, 5491-5496.
37. Vinson, C. R., Sigler, P. B., & McKnight, S. L. (1989) Science 246, 911-916.
38. Vinson, C. R., Hai, T. W., & Boyd, S. M. (1993) Genes Dev. 7, 1047-1058.
39. Zamyatnin, A. (1984) Annu. Rev. Biophys. Bioeng. 13, 145-165.
40. Zhou, N., Kay, C., & Hodges, R. (1992a) Biochemistry 31, 5739-5746.
41. Zhou, N., Kay, C., & Hodges, R. (1992b) J. Biol. Chem. 267, 2664-2670.
42. Zhou, N., Kay, C., & Hodges, R. (1993) Biochemistry 32, 3178-3187.
43. Zhu, B., Zhou, N., Kay, C., & Hodges, R. (1993) Protein Sci. 2, 383-394.