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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
2010-5-20
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pubmed:databankReference |
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pubmed:abstractText |
Diarylpyrimidine (DAPY) non-nucleoside reverse transcriptase inhibitors (NNRTIs) have inherent flexibility, helping to maintain activity against a wide range of resistance mutations. Crystal structures were determined with wild-type and K103N HIV-1 reverse transcriptase with etravirine (TMC125) and rilpivirine (TMC278). These structures reveal a similar binding mode for TMC125 and TMC278, whether bound to wild-type or K103N RT. Comparison to previously published structures reveals differences in binding modes for TMC125 and differences in protein conformation for TMC278.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1520-4804
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
27
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pubmed:volume |
53
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4295-9
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pubmed:meshHeading |
pubmed-meshheading:20438081-Binding Sites,
pubmed-meshheading:20438081-Crystallography, X-Ray,
pubmed-meshheading:20438081-Drug Design,
pubmed-meshheading:20438081-HIV Reverse Transcriptase,
pubmed-meshheading:20438081-HIV-1,
pubmed-meshheading:20438081-Models, Molecular,
pubmed-meshheading:20438081-Mutation,
pubmed-meshheading:20438081-Nitriles,
pubmed-meshheading:20438081-Protein Binding,
pubmed-meshheading:20438081-Protein Conformation,
pubmed-meshheading:20438081-Pyridazines,
pubmed-meshheading:20438081-Pyrimidines
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pubmed:year |
2010
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pubmed:articleTitle |
Crystal structures of HIV-1 reverse transcriptase with etravirine (TMC125) and rilpivirine (TMC278): implications for drug design.
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pubmed:affiliation |
Gilead Sciences, Inc., 333 Lakeside Drive, Foster City, California 94404, USA. eric.lansdon@gilead.com
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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