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HIV-1 protease variants from 100-fold drug resistant clinical isolates: expression, purification, and crystallization

  1. Author:
    Vickrey, J. F.
    Logsdon, B. C.
    Proteasa, G.
    Palmer, S.
    Winters, M. A.
    Merigan, T. C.
    Kovari, L. C.

  2. Author Address

    Wayne State Univ, Sch Med, Dept Biochem & Mol Biol, 540 E Canfield Ave, Detroit, MI 48201 USA Wayne State Univ, Sch Med, Dept Biochem & Mol Biol, Detroit, MI 48201 USA NCI, HIV Drug Resistance Program, NIH, Frederick, MD 21702 USA Stanford Univ, Ctr AIDS Res, Stanford, CA 94305 USA Kovari LC Wayne State Univ, Sch Med, Dept Biochem & Mol Biol, 540 E Canfield Ave, Detroit, MI 48201 USA
    1. Year: 2003
  2. Journal: Protein Expression and Purification
    1. 28
    2. 1
    3. Pages: 165-172
  4. Type of Article: Article
  1. Abstract:

    High-resolution X-ray crystallographic structures of HIV-1 protease clinical variants complexed with licensed inhibitors are essential to understanding the fundamental cause of protease drug resistance. There is a need for structures of naturally evolved HIV-1 proteases from patients failing antiretroviral therapy. Here, we report the expression, purification, and crystallization of clinical isolates of HIV-1 protease that have been characterized to be more than 100 times less susceptible to US FDA approved protease inhibitors. (C) 2002 Elsevier Science (USA). All rights reserved.

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