Viral proteases as targets for chemotherapeutic intervention.
Many viruses encode proteinases that are essential for infectivity, and are consequently attractive chemotherapeutic targets. The biochemistry and structure of the human immunodeficiency virus proteinase have been characterized extensively, and potent peptide-mimetic inhibitors have been developed. Techniques and strategies used to improve the efficiency of these compounds are likely to be applicable to other viral proteinases.
Department of Microbiology, State University of New York, Stony Brook 11794-8621.
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D000595:Amino Acid Sequence; D000818:Animals; D000998:Antiviral Agents / Q000138:chemical synthesis / Q000494:pharmacology*; D004267:DNA Viruses / Q000187:drug effects / Q000201:enzymology*; D015195:Drug Design; D016333:HIV Protease / Q000378:metabolism*; D017320:HIV Protease Inhibitors / Q000138:chemical synthesis / Q000494:pharmacology*; D015497:HIV-1 / Q000187:drug effects / Q000201:enzymology*; D006801:Humans; D008969:Molecular Sequence Data; D017955:Poliovirus / Q000201:enzymology*; D011480:Protease Inhibitors / Q000138:chemical synthesis / Q000494:pharmacology*; D012328:RNA Viruses / Q000187:drug effects / Q000201:enzymology*; D013379:Substrate Specificity
D000998:Antiviral Agents; D017320:HIV Protease Inhibitors; D011480:Protease Inhibitors; D016333:HIV Protease