Viruses 2009, 1(3), 1110-1136; doi:10.3390/v1031110

HIV-1 Protease: Structural Perspectives on Drug Resistance

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Received: 1 October 2009; in revised form: 30 November 2009 / Accepted: 1 December 2009 / Published: 3 December 2009
(This article belongs to the Special Issue Retroviral Enzymes)
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Abstract: Antiviral inhibitors of HIV-1 protease are a notable success of structure-based drug design and have dramatically improved AIDS therapy. Analysis of the structures and activities of drug resistant protease variants has revealed novel molecular mechanisms of drug resistance and guided the design of tight-binding inhibitors for resistant variants. The plethora of structures reveals distinct molecular mechanisms associated with resistance: mutations that alter the protease interactions with inhibitors or substrates; mutations that alter dimer stability; and distal mutations that transmit changes to the active site. These insights will inform the continuing design of novel antiviral inhibitors targeting resistant strains of HIV.
Keywords: protease inhibitors; drug resistance; aspartic protease; molecular mechanism; darunavir
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MDPI and ACS Style

Weber, I.T.; Agniswamy, J. HIV-1 Protease: Structural Perspectives on Drug Resistance. Viruses 2009, 1, 1110-1136.

AMA Style

Weber IT, Agniswamy J. HIV-1 Protease: Structural Perspectives on Drug Resistance. Viruses. 2009; 1(3):1110-1136.

Chicago/Turabian Style

Weber, Irene T.; Agniswamy, Johnson. 2009. "HIV-1 Protease: Structural Perspectives on Drug Resistance." Viruses 1, no. 3: 1110-1136.

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