Ionization states of the catalytic residues in HIV-1 protease

Nature Structural Biology

Volumn 3, Issue 11, 1996, Pages 946-950

  Smith, Ross ^a   Brereton, Ian M ^a   Chai, Richard Y ^b   Kent, Stephen B H ^b  

^a UNIVERSITY OF QUEENSLAND   (Australia)

^b SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEINASE; VIRUS ENZYME;

ARTICLE; CATALYSIS; ENZYME ANALYSIS; ENZYME SYNTHESIS; HUMAN IMMUNODEFICIENCY VIRUS 1; IONIZATION; NONHUMAN; PRIORITY JOURNAL;

ASPARTIC ACID; CATALYSIS; HIV PROTEASE; HIV PROTEASE INHIBITORS; HIV-1; HUMANS; HYDROGEN-ION CONCENTRATION; IONS; MAGNETIC RESONANCE SPECTROSCOPY; PEPSTATINS;

HUMAN IMMUNODEFICIENCY VIRUS; HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 0029859529     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb1196-946     Document Type: Article

References (29)

1. Ratner, L. et al. Complete nucleotide sequence of the AIDS virus, HTLV-III. Nature 313, 277-284 (1985).
2. Oroszlan, S. in Viral Proteinases as Targets For Chemotherapy (Eds H. Kräusslich, S. Oroszlan, E. Wimmer) 87-100 (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, 1989).
3. McQuade, T.J. et al. A synthetic HIV-1 protease inhibitor with antiviral activity arrests HIV-like particle maturation. Science 247, 454-456 (1990).
4. Huff, J.R. HIV protease: a novel chemotherapeutic target for AIDS. J. Med. Chem. 34, 2305-2314 (1991).
5. Cohen, J. Results on new AIDS drugs bring cautious optimism. Science. 271, 755-756 (1996).
6. FDA Press Release (#95-10), 7 December (1995); and, (#96-4), 1 March (1996).
7. Rose, R.E. et al. Human immunodeficiency virus type 1 viral background plays a major role in development of resistance to proteinase inhibitors. Proc. Natl. Acad. Sci. USA 93, 1648-1653 (1996).
8. Condra, J.H. et al. In vivo emergence of HIV-1 variants resistant to multiple protease inhibitors. Nature 374, 569-571 (1995).
9. Hartsuck, J.A. & Tang, J. The carboxylate ion in the active center of pepsin. J. Biol. Chem. 247, 2575-2580 (1972).
10. Pearl, L.H. & Taylor, W.R. A structural model for the retroviral proteases. Nature 329, 351-354 (1987).
11. Pretsch, E., Clerc, T., Seibl, J. & Simon, W. Spectral Data for Structure Determination of Organic Compounds (Springer-Verlag, Berlin, 1989).
12. Holladay, M.W., Salituro, F.G. & Rich, D.H. Synthetic and enzyme inhibition studies of pepstatin analogues containing hydroxyethylene and ketomethylene dipeptide isosteres. J. Med. Chem. 30, 374-383 (1987).
13. Toth, M.V. & Marshall, G.R. A simple, continuous fluorometric assay for HIV protease. Int. J. Pept. Protein. Res. 36, 544-550 (1990).
14. Hyland, L.J., Tomaszek, T.A. & Meek, T.D. Human immunodeficiency virus-1 protease. 2. Use of pH rate studies and solvent kinetic isotope effects to elucidate details of chemical mechanism. Biochemistry 30, 8454-8463 (1991).
15. Furfine, E.S. et al. Two-step binding mechanism for HIV protease inhibitors. Biochemistry 31, 7886-7891 (1992).
16. Yamazaki, T. et al. NMR and X-ray evidence that the HIV protease catalytic aspartyl groups are protonated in the complex formed by the protease and a non-peptide cyclic urea-based inhibitor. J. Amer. Chem. Soc 116, 10791-10792 (1994).
17. Fitzgerald, P.M.D. et al. Crystallographic analysis of a complex between human immunodeficiency virus type 1 protease and acetyl-pepstatin at 2.0-Å resolution. J. Biol. Chem. 265, 14209-14219 (1990).
18. McDaniel, D.H. & Brown, H.C. Hydrogen bonding as a factor in the ionization of dicarboxylic acids. Science 118, 370-374 (1953).
19. Frey, P.A., Whitt, S.A. & Tobin, J.B. A low-barrier hydrogen bond in the catalytic triad of serine proteinases. Science 264, 1927-1930 (1994).
20. Marciniszyn, J.A., Hartsuck, J.A. & Tang, J.J. Mode of inhibition of acid proteases by pepstatin. J. Biol. Chem. 251, 7088-7094 (1976).
21. Marshall, G.R. Structure-activity relations of antagonists of the renin-angiotensin system. Fed. Proc. 35, 2494-2501 (1976).
22. Suguna, K., Padlan, E.A., Smith, C.W., Carlson, W.D. & Davies, D.R. Binding of a reduced bond peptide inhibitor to the aspartic proteinase from rhizopus chinesis: implications for a mechanism of action. Proc. Natl. Acad. Sci. USA 84, 7009-7013 (1937).
23. Schnölzer, M. & Kent, S.B.H. Constructing proteins by dovetailing unprotected synthetic peptides: backbone-engineered HIV protease. Science 256, 221-225 (1992).
24. Toth, G. & Penke, B. An improved method for the preparation of omega-cyclohexyl esters of aspartic and glutamic acid. Synthesis 361-362 (1992).
25. Schnölzer, M., Alewood, P., Jones, A., Alewood, D. & Kent, S.B.H. In situ neutralization in Boc-chemistry solid phase peptide synthesis: rapid, high yield assembly of difficult sequences. Int. J. Pept. Protein Res. 40, 180-193 (1992).
26. Grant, S.K. et al. Use of protein folding studies to determine the conformational and dimer stabilities of HIV-1 and SIV proteases. Biochemistry 31, 9491-9501 (1992).
27. Wlodawer, A. et al. Conserved folding in retroviral proteases: crystal structure of a synthetic HIV-1 protease. Science 245, 616-621 (1989).
28. Mildner, A.M. et al. The HIV-1 protease as enzyme and substrate: mutagenesis of autolysis sites and generation of a stable mutant with retained kinetic properties. Biochemistry 33, 9405-9413 (1994).
29. Bergman, D.A. et al. Kinetic properties of HIV-1 protease produced by total chemical synthesis with cysteine residues replaced by isosteric L-α-n-butyric acid. Lett. Pept. Sci. 2, 99-107 (1995).