Substrate envelope and drug resistance: crystal structure of RO1 in complex with wild-type human immunodeficiency virus type 1 protease

Antimicrob Agents Chemother. 2006 Apr;50(4):1518-21. doi: 10.1128/AAC.50.4.1518-1521.2006.

Abstract

In our previous crystallographic studies of human immunodeficiency virus type 1 (HIV-1) protease-substrate complexes, we described a conserved "envelope" that appears to be important for substrate recognition and the selection of drug-resistant mutations. In this study, the complex of HIV-1 protease with the inhibitor RO1 was determined and comparison with the substrate envelope provides a rationale for mutational patterns.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Crystallography
  • Dipeptides / chemistry*
  • Dipeptides / pharmacology
  • Drug Resistance, Viral
  • HIV Protease / chemistry*
  • HIV Protease Inhibitors / chemistry*
  • HIV Protease Inhibitors / pharmacology
  • Hydrogen Bonding

Substances

  • Dipeptides
  • HIV Protease Inhibitors
  • RO1 compound
  • HIV Protease