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Crystal structure of feline immunodeficiency virus protease--a model for HIV drug resistance.

Gustchina A, Reshetnikova L, Lubkowski J, Zdanov A, Hui KY, Angleton EL, Farmerie WG, Bhatt D, Dunn BM, Wlodawer A.

Abstr Meet Groups Stud Struct AIDS Relat Syst Their Appl Target Drug Des. 1995 Jun 5-7; 9: (unnumbered abstract).

NCI-FCRDC, ABL-BRP, Frederick, MD, USA.

Proteases encoded by retroviruses represent targets for anti-viral therapies. Feline immunodeficiency virus protease (FIV PR) shares many structural similarities with proteases of human and simian immunodeficiency viruses (HIV and SIV), and of Rous sarcoma virus (RSV). The length of its polypeptide chain is intermediate between HIV and RSV PRs. At least four amino acids present in FIV PR are identical to their stereochemical equivalents in drug-resistant mutants of HIV-1 PR. The enzyme is weakly blocked by most potent and specific HIV PR inhibitors. The structural study of complexes of FIV PR with inhibitors will help in understanding the molecular basis of drug resistance for HIV-PR and will open a possibility of direct testing new inhibitors in small animal system. Crystals of FIV PR complexes with statine-based inhibitors (LP-149, LP-130 and LP-123) were grown at 4 degrees C by vapor diffusion with MPD as precipitant, at pH 6.4-7.2. Crystals diffracting up to 1.9 A belong to the space group P3(1)21 (a = b = 50.65 A and c = 74.5 A). The structure of the complex of FIV PR with a hexapeptide statine-based inhibitor, LP-149 (Ki = 260 nM) has been solved using the methods of molecular (MR) and multiple isomorphous replacement (MIR) at 2 A resolution, and was refined to a crystallographic R-factor of 0.148. MR solution utilized a homology-based model of FIV PR, as well as the crystal structures of HIV and RSV PRs. Since the asymmetric unit of crystal contained one half of protease dimer, the inhibitor molecule is two-fold disordered with equal occupancy.

Publication Types:
  • Meeting Abstracts
Keywords:
  • AIDS Vaccines
  • Acquired Immunodeficiency Syndrome
  • Animals
  • Aspartic Endopeptidases
  • Crystallization
  • Drug Resistance
  • Endopeptidases
  • FIV protease
  • Feline Acquired Immunodeficiency Syndrome
  • HIV
  • HIV Infections
  • HIV Protease Inhibitors
  • HIV Seropositivity
  • HIV-1
  • Humans
  • Immunodeficiency Virus, Feline
  • LP 149
  • Models, Biological
  • Oligopeptides
  • Peptide Hydrolases
  • Simian Acquired Immunodeficiency Syndrome
  • Simian immunodeficiency virus
  • organization & administration
Other ID:
  • 96095594
UI: 102215201

From Meeting Abstracts




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