Solution NMR evidence that the HIV-1 protease catalytic aspartyl groups have different ionization states in the complex formed with the asymmetric drug KNI-272

Biochemistry

Volumn 35, Issue 31, 1996, Pages 9945-9950

  Wang, Yun Xing ^a   Freedberg, Darón I ^a   Yamazaki, Toshimasa ^a   Wingfield, Paul T ^b   Stahl, Stephen J ^b   Kaufman, Joshua D ^b   Kiso, Yoshiaki ^c   Torchia, Dennis A ^a  

^a NATIONAL INSTITUTES OF HEALTH   (United States)

^b NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES   (United States)

^c KYOTO PHARMACEUTICAL UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

KYNOSTATIN 272; PROTEINASE; PROTEINASE INHIBITOR;

ARTICLE; DRUG BINDING SITE; DRUG DESIGN; ENZYME ANALYSIS; IONIZATION; NUCLEAR MAGNETIC RESONANCE; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTON NUCLEAR MAGNETIC RESONANCE; PROTON TRANSPORT;

AMINO ACID SEQUENCE; ASPARTIC ACID; BINDING SITES; HIV PROTEASE; HIV PROTEASE INHIBITORS; HIV-1; HUMANS; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; MUTAGENESIS, SITE-DIRECTED; OLIGOPEPTIDES; POINT MUTATION; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; UREA;

HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 0029757151     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi961268z     Document Type: Article

References (19)

1. Baldwin, E. T., Bhat, T. N., Gulnik, S., Liu, B., Topol, I. A., Kiso, Y., Mimoto, T., Mitsuya, H., & Erickson, J. W. (1995) Structure 3, 581-590.
2. Bundi, A., & Wüthrich, K. (1979) Biopolymers 18, 285-297.
3. Burgering, M. J. M., Boelens, R., Caffrey, M., Breg, J. N., & Kaptein, R. (1993) FEBS Lett. 330, 105-109.
4. Chokeijichai, S., Shirasaka, T., Weinstein, J. N., & Mitsuya, H. (1995) Antiviral Res. 28, 25-38.
5. Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., & Bax, A. (1995) J. Biomol. NMR 6, 277-293.
6. Harte, W. E., Jr., & Beveridge, D. L. (1993) J. Am. Chem. Soc. 115, 3883-3886.
7. Huff, J. R. (1991) J. Med. Chem. 34, 2305-2314.
8. Ikura, M., & Bax, A. (1992) J. Am. Chem. Soc. 114, 2433-2440.
9. Kageyama, S., Mimoto, T., Murakawa, Y., Nomizu, M., Ford, H. J., Jr., Shirasaka, T., Gulnik, S., Erickson, J., Takada, K., Hayashi, H., Broder, S., Kiso, Y., & Mitsuya, H. (1993) Antimicrob. Agents Chemother. 37, 810-817.
10. Kiso, Y. (1996) Biopolymers (in press).
11. Ladner, H. K., Led, J. J., & Grant, D. M. (1975) J. Magn. Reson. 20, 530-534.
12. Lam, P. Y., Jadhav, P. K., Eyermann, C. J., Hodge, C. N., Ru, Y., Bacheler, L. T., Meek, J. L., Otto, M. J., Rayner, M. M., Waong, Y. N., Chang, C.-H., Weber, P. C., Jackson, D. A., Sharpe, T. R., & Erickson-Viitanen, S. (1994) Science (Washington, D. C.) 263, 380-384.
13. Led, J. J., & Petersen, S. B. (1979) J. Magn. Reson. 33, 603-617.
14. Oda, Y., Yamazaki, T., Nagayama, K., Kanaya, S., Kuroda, Y., & Nakaumra, H. (1993) Biochemistry 33, 5275-5284.
15. Wlodawer, A., & Erickson, J. W. (1993) Annu. Rev. Biochem. 62, 543-585.
16. Wlodawer, A., Miller, M., Jaskolski, M., Sathyanrayana, B. K., Baldwin, E., Weber, I. T., Selk, L. M., Clawson, L., Schneider, J., & Kent, S. B. H. (1989) Science (Washington, D. C.) 245, 616-621.
17. Yamazaki, T., Nicholson, L., Torchia, D. A., Stahl, S. J., Kaufman, J. D., Wingfield, P. T., Domaille, P. J., & Campbell-Burk, S. (1994a) Eur. J. Biochem. 219, 707-712.
18. Yamazaki, T., Nicholson, L. K., Wingfield, P. T., Stahl, S. J., Haufman, J. D., Lam, P. Y. S., Ru, Y., Jadhav, P. K., Chang, C.-H., Weber, P. C., & Torchia, D. A. (1994b) J. Am. Chem. Soc. 116, 10791-10792.
19. Yamazaki, T., Hinck, A. P., Wang, Y.-X., Nicholson, L. K., Torchia, D. A., Wingfield, P. T., Stahl, S. J., Kaufman, H. D., Chang, C.-H., Domaille, P. J., & Lam, P. Y. S. (1996) Protein Sci. 5, 495-506.