X-Ray Analysis of HIV-1 Protease and Its Complexes with Inhibitors

  • Maria Miller
  • Amy L. Swain
  • Mariusz Jaskólski
  • Bangalore K. Sathyanarayana
  • Garland R. Marshall
  • Daniel Rich
  • Stephen B. H. Kent
  • Alexander Wlodawer
Chapter

Abstract

The HIV-1 protease is essential for the replication of infective virus (Kohl et al., 1988), and is therefore an attractive target for the design of specific inhibitors as potential antiviral therapeutics. The rational design of drugs that can inhibit the action of viral proteases depends on obtaining accurate structures of these enzymes. Chemically synthesized HIV-1 protease (Schneider and Kent, 1988; Merrifield, 1963; Kent, 1988; Tarn et al., 1986) was used to solve crystal structures of unliganded enzyme and of complexes with two peptide inhibitors. The amino acid sequence of the enzyme, corresponding to the SF2 isolate is shown on Figure 1.

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Copyright information

© Macmillan Publishers Limited 1990

Authors and Affiliations

  • Maria Miller
  • Amy L. Swain
  • Mariusz Jaskólski
  • Bangalore K. Sathyanarayana
  • Garland R. Marshall
  • Daniel Rich
  • Stephen B. H. Kent
  • Alexander Wlodawer

There are no affiliations available

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