Crystal structure implies that cyclophilin predominantly catalyzes the Trans to Cis isomerization

Biochemistry

Volumn 35, Issue 23, 1996, Pages 7356-7361

  Zhao, Yingdong ^a   Ke, Hengming ^a  

^a UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOPHILIN A; RECOMBINANT CYCLOPHILIN A; TETRAPEPTIDE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CIS TRANS ISOMERISM; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME SUBSTRATE COMPLEX; HYDROGEN BOND; PRIORITY JOURNAL; STOICHIOMETRY;

AMINO ACID ISOMERASES; AMINO ACID SEQUENCE; BINDING SITES; CARRIER PROTEINS; COMPUTER GRAPHICS; COMPUTER SIMULATION; CYCLOSPORINS; HUMANS; HYDROGEN BONDING; ISOMERISM; KINETICS; MACROMOLECULAR SUBSTANCES; MODELS, MOLECULAR; MODELS, STRUCTURAL; MOLECULAR SEQUENCE DATA; PEPTIDYLPROLYL ISOMERASE; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY;

EID: 0029982651     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9602775     Document Type: Article

References (50)

1. Bächinger, H. P. (1987) J. Biol Chem. 262, 17144-17148.
2. Baker, E. K., Colley, N. J., & Zuker, C. S. (1994) EMBO J. 13, 4886-4895.
3. Brünger, A. T., Kuriyan, J., & Karplus, M. (1987) Science 235, 458-460.
4. Davis, J. M., Boswell, B. A., & Bächinger, H. P. (1989) J. Biol. Chem. 264, 8956-8962.
5. Fischer, G., Wittmann-Liebold, B., Lang, K., Kiefhaber, T., & Schmid, F. X. (1989) Nature 337, 476-478.
6. Franke, E. K., Yuan, H. E. H., & Luban, J. (1994) Nature 372, 359-362.
7. Fransson, C., Freskgård, P., Herbertsson, H., Johansson, Å, Jonasson, P., Moørtensson, L., Svensson, M., Jonsson, B., & Carlsson, U. (1992) FEBS Lett. 296, 90-94.
8. Freskgård, P., Bergenhem, N., Jonsson, B., Svensson, M., & Carlsson, U. (1992) Science 258, 466-468.
9. Fruman, D. A., Klee, C. B., Bierer, B. E., & Burakoff, S. J. (1992) Proc. Natl. Acad. Sci. U.S.A. 89, 3686-3690.
10. Grathwohl, C., & Wüthrich, K. (1981) Biopolymers 20, 2623-2633.
11. Haddy, A., Swanson, S. K. H., Born, T. L., & Rusnak, F. (1992) FEBS Lett. 314, 37-40.
12. Haldane, J. B. S. (1930) Enzyme, Longmans,
13. Handschumacher, R. E., Harding, M. W., Rice, J., & Drugge, R. J. (1984) Science 226, 544-547.
14. Harrison, R. K., & Stein, R. L. (1990a) Biochemistry 29, 1684-1689.
15. Harrison, R. K., & Stein, R. L. (1990b) Biochemistry 29, 3813-3816.
16. Jackson, S. E., & Fersht, A. R. (1991) Biochemistry 30, 10436-10443.
17. Johnson, J. L., & Toft, D. O. (1994) J. Biol. Chem. 269, 24989-24993.
18. Jones, T. A. (1982) in Computational crystallography (Sayre, D., Ed.), pp 303-317, Oxford, London.
19. Kakalis, L. T., & Armitage, I. M. (1994) Biochemistry 33, 1495-1501.
20. Kallen, J., & Walkinshaw, M. D. (1992) FEBS Lett. 300, 286-290.
21. Kallen, J., Spitzfaden, C., Zurini, M. G. M., Wider, G., Widmer, H., Wüthrich, K., & Walkinshaw, M. D. (1991) Nature 353, 276-279.
22. Ke, H. M. (1992) J. Mol. Biol. 228. 539-550.
23. Ke, H. M., Zydowsky, L. D., Liu, J., & Walsh, C. T. (1991) Proc. Natl. Acad. Sci. U.S.A. 88, 9483-9487.
24. Ke, H. M., Mayrose, D., & Cao, W. (1993a) Proc. Natl. Acad. Sci. U.S.A. 90, 3324-3328.
25. Ke, H. M., Zhao, Y., Luo, F., Weissman, I., & Friedman, J. (1993b) Proc. Natl. Acad. Sci. U.S.A., 90, 11850-11854.
26. Ke, H. M., Mayrose, D., Belshaw, P. I., Alberg, D. G., Schreiber, S. T., Chang, Z. Y., Etzkorn, F. A., Ho., S., & Walsh, C. T. (1994) Structure 2, 33-44.
27. Kern, D., Kern, G., Scherer, G., Fischer, G., & Drakenberg, T. (1995) Biochemistry 34, 13594-13602.
28. Kiefhaber, T., Quaas, R., Hahn, U., & Schmid, F. X. (1990) Biochemistry 29, 3053-3061.
29. Klee, C. B., Draetta, G. F., & Hubbard, M. J. (1988) Adv. Protein Chem. 61, 149-199.
30. Kofron, J. L., Kuzmic, P., Kichore, V., Colon-Bonilla, E., & Rieh, D. H. (1991) Biochemistry 30, 6127-6134.
31. Lang, K., Schmid, F. X., & Fischer, G. (1987) Nature 329, 268-270.
32. Liu, J., Albers, M. W., Chen, C. M., Schreiber, S. L., & Walsh, C. T. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 2304-2308.
33. Liu, J., Farmer, J. D., Jr., Lane, W. S., Friedman, J., Weissman, L, & Schreiber, S. L. (1991) Cell 66, 807-815.
34. Mikol, V., Kallen, J., Pflügl, G., & Walkinshaw, M. D. (1993) J. Mol. Biol. 234, 1119-1130.
35. Mikol, V., Kallen, J., & Walkinshaw, M. D. (1994) Proc. Natl. Acad. Sci. U.S.A. 91, 5183-5186.
36. Navaza, J. (1994) Acta Crystallogr. A50, 157-163.
37. Pflügl, G., Kallen, J., Schirmer, T., Jansonius, J. N., Zurini, M. G. M., & Walkinshaw, M. D.,(1993) Nature 361, 91-94.
38. Radzacki, A., Acheson, S. A., & Wolfenden, R. (1992) Bioorg. Chem. 20, 382-386.
39. Ramachandran, G. N., & Sasisekharan, V. (1968) Conformation of polypeptide and proteins, Adv. Protein Chem. 23, 283-437.
40. Schönbrunner, E. R., Mayer, S., Tropschug, M., Fischer, G., Takahashi, N., & Schmid, F. X. (1991) j. Biol. Chem. 266, 3630-3635.
41. Schutkowski, M., Wöllner, S., & Fischer, G. (1995) Biochemistry 34, 13016-13026.
42. Stein, R. L. (1993) Adv. Protein Chem. 44, 1-23.
43. Steinmann, B., Bruchner, P., & Superti-Furga, A. (1991) J. Biol. Chem. 266, 1299-1303.
44. Swanson, S. K. H., Born, T., Zydowsky, L. D., Cho, H., Chang, H. Y., Walsh, C. T., & Rusnak, F. (1992) Proc. Natl. Acad. Sci. U.S.A. 89, 3741-3745.
45. Takahashi, N., Hayano, T., & Suzuki, M. (1989) Nature 337,473-475.
46. Thall, M., Bukovsky, A., Kondo. E., Rosenwirth, B., Walsh, C. T., Sodroski, J., & Göttlinger, H. G. (1994) Nature 372, 363-365.
47. Thériault, Y., Logan, T. M., Meadows, R., Yu, L., Olejniczak, E. T., Holzman,T. F., Simmer, R. L., & Fesik, S. W. (1993) Nature 361, 88-91.
48. Wolfenden, R., & Radzacki, A. (1991) Chemtracts 2, 52-54.
49. Zhao, Y., & Ke, H. (1996) Biochemistry 35, 7362-7368.
50. Zydowsky, L. D., Etzkorn, F. A., Chang, H. Y., Ferguson, S. B., Stolz, L. A., Ho, S. I., & Walsh, C. T. (1992) Protein Sci. 1, 1092-1099.