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Structural and biochemical studies of retroviral proteases

  1. Author:
    Wlodawer, A.
    Gustchina, A.

  2. Author Address

    Wlodawer A NCI, Frederick Canc Res & Dev Ctr, Program Struct Biol, Macromol Crystallog Lab Frederick, MD 21702 USA NCI, Frederick Canc Res & Dev Ctr, Program Struct Biol, Macromol Crystallog Lab Frederick, MD 21702 USA
    1. Year: 2000
  2. Journal: Biochimica et Biophysica Acta - Protein Structure & Molecular Enzymology
    1. 1477
    2. 1-2
    3. Pages: 16-34
  4. Type of Article: Review
  1. Abstract:

    Retroviral proteases form a unique subclass of the family of aspartic proteases. These homodimeric enzymes from a number of viral sources have by now been extensively characterized, both structurally and biochemically. The importance of such knowledge to the development of new drugs against AIDS has been, to a large extent, the driving force behind this progress. High-resolution structures are now available for enzymes from human immunodeficiency virus types 1 and 2. simian immunodeficiency virus. feline immunodeficiency virus, Rous sarcoma virus. and equine infectious anemia virus. In this review. structural and biochemical data for retroviral protrases are compared in order to analyze the similarities and differences between the enzymes from different sources and to enhance our understanding of their propel-ties. (C) 2000 Elsevier Science B.V. All rights reserved. [References: 107]

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