Crystal structures of HIV-1 reverse transcriptase with etravirine (TMC125) and rilpivirine (TMC278): implications for drug design.

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 Lansdon EB2010 Reverse Transcriptase Activity Yes
HIV RT Lansdon EB2010 Reverse Transcriptase Activity No
HIV RT Lansdon EB2010 Associated condition HIV

Structures:

3MEG 3MEE 3MED 3MEC
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