Crystallographic analysis of the binding modes of thiazoloisoindolinone non-nucleoside inhibitors to HIV-1 reverse transcriptase and comparison with modeling studies

J Med Chem. 1999 Sep 23;42(19):3845-51. doi: 10.1021/jm990275t.

Abstract

We have determined the crystal structures of thiazoloisoindolinone non-nucleoside inhibitors in complex with HIV-1 reverse transcriptase to high-resolution limits of 2.7 A (BM +21.1326) and 2. 52 A (BM +50.0934). We find that the binding modes of this series of inhibitors closely resemble that of "two-ring" non-nucleoside reverse transcriptase inhibitors. The structures allow rationalization of stereochemical requirements, structure-activity data, and drug resistance data. Comparisons with our previous structures suggest modifications to the inhibitors that might improve resilience to drug-resistant mutant forms of reverse transcriptase. Comparison with earlier modeling studies reveals that the predicted overlap of thiazoloisoindolinones with TIBO was largely correct, while that with nevirapine was significantly different.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallography, X-Ray
  • HIV Reverse Transcriptase / antagonists & inhibitors*
  • HIV Reverse Transcriptase / metabolism*
  • Indoles / chemistry*
  • Indoles / metabolism*
  • Models, Chemical
  • Models, Molecular
  • Protein Binding
  • Protein Conformation
  • Reverse Transcriptase Inhibitors / chemistry*
  • Reverse Transcriptase Inhibitors / metabolism*
  • Structure-Activity Relationship
  • Thiazoles / chemistry*
  • Thiazoles / metabolism*

Substances

  • BM 21.1326
  • BM 50.0934
  • Indoles
  • Reverse Transcriptase Inhibitors
  • Thiazoles
  • HIV Reverse Transcriptase