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Persistent URL
http://purl.org/net/epubs/work/66063
Record Status
Checked
Record Id
66063
Title
Joint X-ray/Neutron Crystallographic Study of HIV-1 Protease with Clinical Inhibitor Amprenavir: Insights for Drug Design
Contributors
IT Weber
,
MJ Waltman
,
M Mustyakimov
,
MP Blakeley
,
DA Keen (STFC Rutherford Appleton Lab.)
,
AK Ghosh
,
P Langan
,
AY 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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ISIS
,
STFC
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Language
English (EN)
Type
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Journal Article
J Med Chem
56, no. 13 (2013): 5631-5635.
doi:10.1021/jm400684f
2013
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