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

    Abstract

    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 1 2011

    Keywords

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

    ASJC Scopus subject areas

    • Chemistry(all)

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