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American Chemical Society, Journal of Medicinal Chemistry, 13(56), p. 5631-5635, 2013

DOI: 10.1021/jm400684f

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Joint X-ray/Neutron Crystallographic Study of HIV-1 Protease with Clinical Inhibitor Amprenavir: Insights for Drug Design

Journal article published in 2013 by It Weber, Mj Waltman, Marat Mustyakimov, Matthew P. Blakeley, Da Keen, Ak Ghosh, Paul Langan ORCID, Ay Kovalevsky
This paper is available in a repository.
This paper is available in a repository.

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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.