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

Year: 2013
Type: article
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.
DOI: 10.1021/jm400684f
Authors: Irene T. Weber, Mary Jo Waltman, Marat Mustyakimov, Matthew P. Blakeley, David A. Keen, Arun K. Ghosh, Paul Langan, Andrey Y. Kovalevsky
Institutions: Georgia State University, Los Alamos National Laboratory, Oak Ridge National Laboratory, Institut Laue-Langevin, Rutherford Appleton Laboratory, Purdue University West Lafayette
Language: English
Open Access status: green
OpenAlex ID: W2013670871
FWCI: 3.307
Cites: 40
Cited by: 72
Related to: 10