Structure-based inhibitors of HIV-1 protease
A Wlodawer, JW Erickson - Annual review of biochemistry, 1993 - annualreviews.org
A Wlodawer, JW Erickson
Annual review of biochemistry, 1993•annualreviews.orgThe human immunodeficiency virus (HIV), the causative agent of AIDS, encodes an aspartic
protease (HIV PR) whose function is essential for proper virion assembly and maturation.
Inactivation of HIV PR by either mutation or chemical inhibition leads to the production of
immature, non-infectious viral particles (1-3). Thus, HIV PR is considered to be a promising
target for the rational design of drugs against AIDS. HIV PR inhibitors represent a new class
of therapeutic agents that complements existing approaches to antiviral therapy that target …
protease (HIV PR) whose function is essential for proper virion assembly and maturation.
Inactivation of HIV PR by either mutation or chemical inhibition leads to the production of
immature, non-infectious viral particles (1-3). Thus, HIV PR is considered to be a promising
target for the rational design of drugs against AIDS. HIV PR inhibitors represent a new class
of therapeutic agents that complements existing approaches to antiviral therapy that target …
The human immunodeficiency virus (HIV), the causative agent of AIDS, encodes an aspartic protease (HIV PR) whose function is essential for proper virion assembly and maturation. Inactivation of HIV PR by either mutation or chemical inhibition leads to the production of immature, non-infectious viral particles (1-3). Thus, HIV PR is considered to be a promising target for the rational design of drugs against AIDS. HIV PR inhibitors represent a new class of therapeutic agents that complements existing approaches to antiviral therapy that target another enzyme, the HIV reverse transcriptase (4). There are several excellent recent reviews on the subject of HIV PR inhibitor structure-activity relationships (5-9).
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