Abstract
The principal pathogen of acquired immunodeficiency syndrome (AIDS) in the United States is human immunodeficiency virus type 1 (HIV-1), but the disease is sometimes caused by a second variant, HIV-2. These two viruses share a similar genomic organization, indicating common evolutionary origin, but differ significantly in terms of nucleotide and amino-acid sequence, with no more than 60% overall amino-acid identity. Elucidation of the structures of virally-encoded enzymes offers an opportunity for rational drug design and has been pursued by many groups. The structure of only one enzyme encoded by HIV-1, that of the aspartyl protease (PR), is currently known (Navia et al., 1989; Wlodawer et al., 1989). This enzyme is essential for viral maturation, and is the target of choice for designing new therapeutic agents.
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© 1991 Plenum Press, New York
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Gustchina, A., Weber, I.T., Wlodawer, A. (1991). Molecular Modeling of the HIV-2 Protease. 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_75
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DOI: https://doi.org/10.1007/978-1-4684-6012-4_75
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