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Mechanism of inhibition of HIV-1 reverse transcriptase by non-nucleoside inhibitors.

Abstract:

The structure of unliganded HIV-1 reverse transcriptase has been determined at 2.35 A resolution and refined to an R-factor of 0.219 (for all data) with good stereochemistry. The unliganded structure was produced by soaking out a weak binding non-nucleoside inhibitor, HEPT, from pregrown crystals. Comparison with the structures of four different RT and non-nucleoside inhibitor complexes reveals that only minor domain rearrangements occur, but there is a significant repositioning of a three-st...

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Publication status:
Published

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Publisher copy:
10.1038/nsb0495-303

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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Biology
Role:
Author
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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Biology
Role:
Author
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Journal:
Nature structural biology
Volume:
2
Issue:
4
Pages:
303-308
Publication date:
1995-04-05
DOI:
ISSN:
1072-8368
URN:
uuid:3c1d9ec8-d640-4be2-aa5d-27eda0b863e7
Source identifiers:
26989
Local pid:
pubs:26989

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