期刊
VIRUSES-BASEL
卷 1, 期 3, 页码 1110-1136出版社
MDPI AG
DOI: 10.3390/v1031110
关键词
protease inhibitors; drug resistance; aspartic protease; molecular mechanism; darunavir
类别
资金
- United States National Institutes of Health [GM062920]
- Georgia State University
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM062920, U01GM062920] Funding Source: NIH RePORTER
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.
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