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A structural model for the retroviral proteases

Nature volume 329, pages 351–354 (1987)Cite this article

Abstract

In many retroviruses the 5' end of the pol gene codes for a protease vital for the processing of the gag polyprotein into the separate core proteins1,2. In some viruses this protease is encoded at the 3' end of the gag gene3, or between the gag and pol genes in a different reading frame to either4. A sequence, Asp-Thr-Gly, which is conserved in retroviral proteases is also conserved in the active sites of aspartic proteases, an observation which has led to the suggestion that the retroviral proteases could belong to this family5,6. We have examined the sequences of the aspartic and retroviral protease families, using pattern-recognition, structure prediction and molecular modelling techniques, and conclude that the viral protease sequences probably correspond to a single domain of an aspartic protease and may function in a dimeric form. We have constructed a model of the pol-protease of human immunodeficiency virus 1 (HIV-1) to test this hypothesis.

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Author information

Author notes

  1. William R. Taylor

    Present address: National Institute for Medical Research, The Ridgeway, Mill Hill, London, NW7 1AA, UK

Authors and Affiliations

  1. Cancer Research Campaign Biomolecular Structure Unit, Institute of Cancer Research, Clifton Ave., Sutton, Surrey, SM2 5PX, UK

    Laurence H. Pearl

  2. Laboratory of Molecular Biology, Dept. of Crystallography, Birkbeck College, University of London, Malet Street, London, WC1E 7HX, UK

    William R. Taylor

Authors
  1. Laurence H. Pearl
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  2. William R. Taylor
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Pearl, L., Taylor, W. A structural model for the retroviral proteases. Nature 329, 351–354 (1987). https://doi.org/10.1038/329351a0

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