| Literature DB >> 31474336 |
Daniel W Kneller1, Johnson Agniswamy1, Arun K Ghosh2, Irene T Weber3.
Abstract
Drug-resistance threatens effective treatment of HIV/AIDS. Clinical inhibitors, including darunavir (1), are ineffective for highly resistant protease mutant PR20, however, antiviral compound 2 derived from 1 with fused tricyclic group at P2, extended amino-benzothiazole P2' ligand and two fluorine atoms on P1 shows 16-fold better inhibition of PR20 enzyme activity. Crystal structures of PR20 and wild-type PR complexes reveal how the extra groups of 2 counteract the expanded ligand-binding pocket, dynamic flaps, and faster dimer dissociation of PR20.Entities:
Keywords: Antiretroviral inhibitor; Drug resistance; HIV protease; Structure-based design; X-ray crystallography
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Year: 2019 PMID: 31474336 PMCID: PMC7251940 DOI: 10.1016/j.bbrc.2019.08.126
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575