期刊
JOURNAL OF MEDICINAL CHEMISTRY
卷 56, 期 13, 页码 5631-5635出版社
AMER CHEMICAL SOC
DOI: 10.1021/jm400684f
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资金
- DOE-OBER
- DOE-BES
- NIH-NIGMS [1R01GM071939-01]
- NIH [R01GM062920, GM053386]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM071939, R01GM053386, R37GM053386, R01GM062920] Funding Source: NIH RePORTER
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 angstrom resolution. The structure provides direct determination of hydrogen en atom positions in enzyme active enzyme-drug interactions suggests that some hydrogen bond's 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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