The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix

Nature Structural Biology

Volumn 7, Issue 2, 2000, Pages 113-117

  Li, Mi ^b   Phylip, Lowri H ^c   Lees, Wendy E ^c   Winther, Jakob R ^d   Dunn, Ben M ^e   Wlodawer, Alexander ^a   Kay, John ^c   Gustchina, Alia ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

^b SAIC FREDERICK INC   (United States)

^c CARDIFF UNIVERSITY   (United Kingdom)

^d CARLSBERG LABORATORY   (Denmark)

^e UNIVERSITY OF FLORIDA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC PROTEINASE; ASPARTIC PROTEINASE INHIBITOR; FUNGAL ENZYME; PEPSIN A;

ALPHA HELIX; ARTICLE; CIRCULAR DICHROISM; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME INHIBITION; ENZYME KINETICS; ENZYME PURIFICATION; ENZYME STRUCTURE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FOLDING; SACCHAROMYCES CEREVISIAE;

AMINO ACID SEQUENCE; ASPARTIC ENDOPEPTIDASES; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; FUNGAL PROTEINS; HYDROGEN-ION CONCENTRATION; METHIONINE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN CONFORMATION; PROTEIN FOLDING; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; TRYPSIN;

SACCHAROMYCES CEREVISIAE;

EID: 0033950453     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/72378     Document Type: Article

References (31)

1. Handbook of proteolytic enzymes (eds Barrett, A.J.. Woessner, J.F. & Rawlings, N.D.) 1-1650 (Academic Press, London; 1998).
2. Schreuder H.A. et al.. Nature Struct. Biol. 1, 48-54 (1994).
3. Engh, R.A. et al. J. Mol. Biol. 234, 1060-1069 (1993).
4. Gomis-Ruth, F.X. et al. Nature, 389, 77-81 (1997).
5. Christeller, J.T., Farley, P. E., Ramsay, R.J., Sullivan, P. A. & Laing, W.A. Eur. J. Biochem. 254, 160-167 (1998).
6. Dreyer, T., Valler, M. J., Kay, J., Chariten, P. & Dunn, B.M. Biochem. J. 231, 777-779 (1985).
7. Craig. C. et al. AIDS 12, 1611-1618(1998).
8. Dame, J.B. et al. Mol. Biochem. Parasitol. 64, 177-190 (1994).
9. Monod, M., Togni, G., Hube, B. & Sanglard, D. Mol. Microbiol. 13, 357-368 (1994).
10. Wlodawer, A. & Vondrasek, J. Annu. Rev. Biophys. Biomol. Struct. 27, 249-284 (1998).
11. Moon, R.P. et al. Eur. J. Biochem. 244, 552-560 (1997).
12. Roberts, N.A., Craig, J.C. & Sheldon, J. AIDS 12, 453-460 (1998).
13. Takahashi, S. et al. J. Biochem. 125, 348-353 (1999).
14. Kageyama. T. Eur. J. Biochem. 253, 804 - 809 (1998).
15. Kreft, S. et al, Phytochemistry 44, 1001-1006 (1997).
16. Saheki, T., Matsuda, Y. & Holzer, H. Eur. J. Biochem. 47, 325-332 (1974).
17. Aguilar, C.F. et al. J. Mol. Biol. 267, 899-915 (1997).
18. Schu, P. & Wolf, D.H. FEBS Lett. 283, 78-84 (1991).
19. Biedermann, K., Montali, U., Martin, B., Svendsen, l. B. & Ottesen, M. Carlsberg Res. Commun. 45, 225-235 (1980).
20. Kondo, H. et al. J. Biochem. 124, 141-147 (1998).
21. Rost, B. & Sander, C J. Mol. Biol. 232, 584-599 (1993).
22. Davies, D.R. Annu. Rev. Biophys. Biophys. Chem. 19, 189-215 (1990).
23. Richter, C., Tanaka, T., Koseki, T. & Yada, R.Y. Eur. J. Biochem. 261, 746-752 (1999).
24. Khan, A.R. & James, M.N.G. Protein Sci. 7, 815-836 (1998).
25. Wu, C.Y., Robertson, D.H.L., Hubbard, S.J., Gaskell, S. J. & Beynon, R. J. J. Biol. Chem. 274, 1108-1115 (1999).
26. Cooper, J.B. et al. Biochemistry 28, 8596-8603 (1989).
27. Tigue, N. J. & Kay, J. J. Biol. Chem. 273, 26441-26446 (1998).
28. Otwinowski, Z. & Minor, W. Methods Enzymol. 276, 307-326 (1997).
29. Navaza, J. Acta Crystallogr. A 50, 157-163 (1994).
30. Jones, T. A. & Kieldgaard, M. Methods Enzymol. 277, 173-208 (1997).
31. Brünger, A. T. et al. Acta Crystallogr. D 54, 905-921 (1998).