Abstract
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.
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