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Persistent URL http://purl.org/net/epubs/work/66063
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Record Id 66063
Title Joint X-ray/Neutron Crystallographic Study of HIV-1 Protease with Clinical Inhibitor Amprenavir: Insights for Drug Design
Contributors
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.
Organisation ISIS , STFC
Keywords ISIS 2013
Funding Information
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Language English (EN)
Type Details URI(s) Local file(s) Year
Journal Article J Med Chem 56, no. 13 (2013): 5631-5635. doi:10.1021/jm400684f 2013
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