X-ray crystal structure and dynamics reveal HIV-1 protease drug interactions

Yong Wang, Tamaria G. Dewdney, Zhigang Liu, Samuel J. Reiter, Joseph S. Brunzelle, Iulia A. Kovari, Ladislau C. Kovari

Research output: Contribution to journalArticlepeer-review

1 Scopus citations


The dynamic movement of HIV-1 protease is an important feature for inhibitor design. The wide-open form of multi-drug resistant HIV-1 protease solved by our group exhibits an increase in flap distance. Stabilizing the protease flaps could be a strategy to overcome drug resistance. A peptidic inhibitor stabilizing the protease-inhibitor complex and a structural novel inhibitor targeting the wide-open form protease have been identified as a new scaffold for drug development.

Original languageEnglish (US)
Pages (from-to)221-230
Number of pages10
JournalStudia Universitatis Babes-Bolyai Chemia
Issue number3
StatePublished - Sep 2011


  • Drug design
  • HIV-1 protease
  • Multi-drug resistance

ASJC Scopus subject areas

  • Chemistry(all)


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