期刊
JOURNAL OF MEDICINAL CHEMISTRY
卷 53, 期 10, 页码 4295-4299出版社
AMER CHEMICAL SOC
DOI: 10.1021/jm1002233
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资金
- Office of Science, Office of Basic Energy Sciences, of the U.S. Department of Energy [DE-AC02-05CH11231]
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 K 103N 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 TM C125 and differences in protein conformation for TMC278.
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