Characterization of HIV-1 protease mutants: random, directed, selected.
The HIV-1 protease is becoming one of the most important proteins in medicine. It is perhaps the most attractive target for development of an anti-HIV-1 therapeutic drug. Given its pre-eminent position in biomedical research, many aspects of the protease are currently coming under close scrutiny. Protease is available from recombinant sources, and numerous structures of the enzyme (with and without bound inhibitors) have now been determined by crystallographic methods, enabling the full utilization of mutational analysis in the study of protease function. In addition, the selection of HIV-1 mutants with reduced sensitivity to protease inhibitors is further complementing research on this enzyme.
Swanstrom
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Department of Biochemistry and Biophysics, UNC Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill 27599-7295.
D004252:DNA Mutational Analysis; D004352:Drug Resistance, Microbial / Q000235:genetics; D016333:HIV Protease / Q000187:drug effects / Q000235:genetics* / Q000378:metabolism; D017320:HIV Protease Inhibitors / Q000494:pharmacology; D015497:HIV-1 / Q000201:enzymology*; D009154:Mutation
D017320:HIV Protease Inhibitors; D016333:HIV Protease