12
Views
3
CrossRef citations to date
0
Altmetric
Original

Understanding HIV protease: Can it be translated into effective therapy against AIDS?

, , , &
Pages 127-135 | Published online: 29 Mar 2011

References

  • Toh H, Ono M, Saigo K, Miyata T. Retroviral protease-like sequence in the yeast uansposon Ty1. Nature 1985; 315: 691
  • Kohl N E, Emini E A, Schleif W A, et al. Active human immunodeficiency virus proteae is required for viral infectivity. Proc Natl Acad Sci USA 1988; 85: 4686–90
  • Wlodawer A, Miller M, Jaskolski M, et al. Conserved folding in reuoviral proteinases: crystal structure of a synthetic HIV-1 protease. Science 1989; 245: 616–21
  • Navia M A, Fitzgerald P MD, McKeever B M, et al. Three-dimentional structure of aspartyl protease from human immunodeficiency virus HIV-1. Nature 1989; 337: 615–20
  • Lapatto R, Blundell T, Hemmings A, et al. X-ray analysis of HIV-1 proteinase at 2.7Å resolution confirms structural homology among retroviral enzymes. Nature 1989; 342: 299–302
  • Petteway S R, Jr, Dreyer G B, Meek T D, Metcalf B W, Lambert DM. HIV-1 protease: Structure-function and inhibition as a potential AIDS therapy. AIDS Research Review, W. C. Koff, F. Wong-Staal, R. C. Kennedy. M. Dekker, New York 1991; 1: 267–88
  • Tomasselli A G, Howe W J, Sawyer T K, Wlodawer A, Heinrikson RL. The complexities of AIDS: an assessment of the HIV protease as a therepeutic target. Chimicaoggi-Chemistry Today 1991; 9: 6–27
  • Graves MC. Human immunodeficiency virus proteinase: Now, then what next?. Structure and Function of the Aspartic Proteinases, B. M. Dunn. Plenum Press, New York. 1991; 395–405
  • Weber I. Comparison of the crystal structures and intersubunit interactions of human immunodeficiency and Rous sarcoma virus proteases. J Biol Chem 1990; 265: 10492–6
  • Davies DR. The structure and function of the aspartic proteinases. Ann Rev Biophys Biophys Chem 1990; 19: 189–215
  • Tang J, James M NG, Hsu I N, Jenkins J A, Blundell TL. Structural evidence for gene duplication in the evolution of the acid proteases. Nature 1978; 271: 618–21
  • Abad-Zapatero C, Rydel T J, Erickson J. Revised 2.3 Å structure of porcine pepsin: evidence for a flexible sub-domain. Proteins 1990; 8: 62–81
  • Cooper J B, Khan G, Taylor G, Tickle I J, Blundell TL. X-ray analyses of aspartic proteinases. Three-dimentional structure of the hexagonal crystal form of porcine pepsin at 2.3Å resolution. J Mol Biol 1990; 214: 199–222
  • Sielecki A R, Fedorov A A, Boodhoo A, Andreeva N S, James M NG. Molecular and crystal structure of monoclinic porcine pepsin refined at 1.8 Å resolution. J Mol Biol 1990; 214: 143–70
  • Goldblum A. Theoretical calculations on the acidity of the active site in aspartic proteinases. Biochemistry 1988; 27: 1653–8
  • Goldblum A. Modulation of the affinity of aspartic proteases by the mutated residues in active site models. FEBS Lett 1990; 261: 241–4
  • Ido E, Han H P, Kezdy F J, Tang J. Kinetic studies of human immuno-deficiency virus type 1 protease and its active-site hydrogen bond mutant A28S. J Biol Chem 1991; 266: 24359–66
  • Lin Y Z, Fusek M, Lin X L, Hartsuck JA, Kezdy F J, Tang J. pH dependence of kinetic parameters of pepsin, Rhizopus-pepsin, and their active-site hydrogen bond mutants, (Submitted for publication.)
  • Tang J, Wong R NS. Evolution in the structure and function of aspartic proteases. J Cell Biochem 1987; 33: 53–63
  • Co E, Koelsch G, Tang J, Ido E. Mechanism of proteolytic processing of an HIV-1 protease precursor. FASEB J 1992; 6: 2638
  • Marciniszyn J, Jr, Hartsuck J A, Tang J. Mechanism of Intramolecular activation of pepsinogen. J Biol Chem 1976; 251: 7088–94
  • Fruton JS. The mechanism of the catalytic action of pepsin and related acid proteinases. Adv Enzymol 1976; 44: 1–36
  • Poorman R A, Tomasselli A G, Heinrikson R L, Kezdy FJ. A cumulative specificity model for proteases from human immunodeficiency virus types 1 and 2, inferred from statistical analysis of an extended substrate data base. J Biol Chem 1991; 266: 14554–61
  • Blumenstein J J, Copeland T D, Oroszlan S, Michejda CJ. Synthetic non-peptide inhibitors of HIV protease. Biochem Biophys Res Commun 1989; 163: 980–7
  • Des Jarlais R L, Seibel G L, Kuntz I D, et al. Structure-based design of nonpeptide inhibitors specific for the human immunodeficiency virus 1 protease. Proc Natl Acad Sci USA 1990; 87: 6644–8
  • Rajagopolan T G, Stein W H, Moore S. The inactivation of pepsin by diazo-acetyl-norleucine methyl ester. J Biol Chem 1966; 241: 4295–7
  • Chen K CS, Tang J. Amino acid sequence around the epoxide-reactive residues in pepsin. J Biol Chem 1972; 247: 2566–74
  • Zhang Z-Y, Poorman R A, Maggiora L L, Heinrikson R L, Kezdy FJ. Dissociative inhibition of dimeric enzymes. Kinetic characterization of the inhibition of HIV-1 protease by its COOH-terminal tetra-peptide. J Biol Chem 1991; 266: 15591–4
  • Baltimore D. Intracellular immunization. Nature 1988; 335: 395–6
  • Babe L M, Pichuantes S, Craik CS. Inhibition of HIV protease activity by heterodimer formation. Biochem 1991; 30: 106–11

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.