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Complexes of HIV-1 reverse transcriptase with inhibitors of the HEPT series reveal conformational changes relevant to the design of potent non-nucleoside inhibitors.

Abstract:

Crystal structures of HIV-1 reverse transcriptase (RT) complexed with a range of chemically diverse non-nucleoside inhibitors (NNIs) have shown a single pocket in which the inhibitors bind and details of the inhibitor-protein interactions. To delineate the structural requirements for an effective inhibitor, we have determined the structures of three closely related NNIs which vary widely in their potencies. Crystal structures of HIV-1 RT complexed with two very potent inhibitors, MKC-442 and ...

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Publication status:
Published

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Publisher copy:
10.1021/jm960056x

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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Biology
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Biology
Role:
Author
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Journal:
Journal of medicinal chemistry
Volume:
39
Issue:
8
Pages:
1589-1600
Publication date:
1996-04-05
DOI:
EISSN:
1520-4804
ISSN:
0022-2623
URN:
uuid:9b2fa6b7-5ef6-4ff4-8090-55e12c2681ba
Source identifiers:
26154
Local pid:
pubs:26154

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