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Mutational analysis of Tyr-318 within the non-nucleoside reverse transcriptase inhibitor binding pocket of human immunodeficiency virus type I reverse transcriptase.

Abstract:

The highly conserved Tyr-318 is part of the non-nucleoside reverse transcriptase inhibitor (NNRTI)-specific lipophilic pocket of human immunodeficiency virus type I reverse transcriptase (RT) and makes contact within 4 A with the NNRTIs in all reported RT/NNRTI complexes. Using site-directed mutagenesis, six mutant RTs were constructed bearing the mutations Y318H, Y318K, Y318L, Y318C, Y318W, and Y318F. We found that only the Y318W and Y318F mutant RTs retained substantial RT activity, whereas...

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Publication status:
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Publisher copy:
10.1074/jbc.273.51.34234

Authors


Pelemans, H More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Biology
Jonckheere, H More by this author
De Clercq, E More by this author
Balzarini, J More by this author
Journal:
The Journal of biological chemistry
Volume:
273
Issue:
51
Pages:
34234-34239
Publication date:
1998-12-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:b65688c4-e285-4781-8fea-6f651c51b9c6
Source identifiers:
22467
Local pid:
pubs:22467

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