Crystal structures of HIV-1 reverse transcriptase with etravirine (TMC125) and rilpivirine (TMC278): implications for drug design.
J Med Chem (2010), Volume 53, Page 4295
Abstract:
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.
Polymerases:
Topics:
Health/Disease, Structure and Structure/Function, Reverse Transcriptase
Status:
| new | topics/pols set | partial results | complete | validated |
Results:
| Polymerase | Reference | Property | Result | Context |
|---|---|---|---|---|
| HIV RT K103N | Crystal structures of HIV-1 reverse transcriptase with etravirine (TMC125) and rilpivirine (TMC278): implications for drug design. | Reverse Transcriptase Activity | Yes | |
| HIV RT | Crystal structures of HIV-1 reverse transcriptase with etravirine (TMC125) and rilpivirine (TMC278): implications for drug design. | Reverse Transcriptase Activity | No | |
| HIV RT | Crystal structures of HIV-1 reverse transcriptase with etravirine (TMC125) and rilpivirine (TMC278): implications for drug design. | Associated condition | HIV |
Entry validated by:
Structures:
