Joint X-ray/Neutron Crystallographic Study of HIV-1 Protease with Clinical Inhibitor Amprenavir: Insights for Drug Design
Journal of Medicinal Chemistry2013Vol. 56(13), pp. 5631–5635
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Irene T. Weber, Mary Jo Waltman, Marat Mustyakimov, Matthew P. Blakeley, David A. Keen, Arun K. Ghosh, Paul Langan, Andrey Kovalevsky
Abstract
HIV-1 protease is an important target for the development of antiviral inhibitors to treat AIDS. A room-temperature joint X-ray/neutron structure of the protease in complex with clinical drug amprenavir has been determined at 2.0 Å resolution. The structure provides direct determination of hydrogen atom positions in the enzyme active site. Analysis of the enzyme-drug interactions suggests that some hydrogen bonds may be weaker than deduced from the non-hydrogen interatomic distances. This information may be valuable for the design of improved protease inhibitors.
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