Abstract
The aspartyl proteinase encoded within the genome of the type I human immunodeficiency virus (HIV-1 PR) is a valid and important target for the development of a therapeutic to treat HIV infections. Progress in this area has been rapid due to 1) the wealth of previous experience with other aspartyl proteinases and 2) the massive commitment by a large number of research groups worldwide. In this chapter we would like to discuss some of our efforts to develop a PR inhibitor by describing the structure of a complex between HIV-1 PR and a hydroxyethylene inhibitor. As a final note before continuing, we would like to acknowledge the significant contributions that Alex Wlodawer and his group have made to this field which have been important to the progress made not only by our group but by many others as well.
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© 1991 Plenum Press, New York
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Graves, B.J. et al. (1991). The Three-Dimensional X-Ray Crystal Structure of HIV-1 Protease Complexed with a Hydroxyethylene Inhibitor. In: Dunn, B.M. (eds) Structure and Function of the Aspartic Proteinases. Advances in Experimental Medicine and Biology, vol 306. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-6012-4_58
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DOI: https://doi.org/10.1007/978-1-4684-6012-4_58
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