3MEG

HIV-1 K103N Reverse Transcriptase in Complex with TMC278

Summary for 3MEG

• Entry DOI: 10.2210/pdb3meg/pdb
• Related: 3MEC 3MED 3MEE
• Descriptor: p66 Reverse transcriptase, p51 Reverse transcriptase, 4-{[4-({4-[(E)-2-cyanoethenyl]-2,6-dimethylphenyl}amino)pyrimidin-2-yl]amino}benzonitrile, ... (5 entities in total)
• Functional Keywords: hiv, reverse transcriptase, tmc278, rilpivirine, nnrti, transferase
• Biological source: HIV-1 M:B_HXB2R (HIV-1); More
• Cellular location: Gag-Pol polyprotein: Host cell membrane; Lipid-anchor . Matrix protein p17: Virion membrane; Lipid- anchor . Capsid protein p24: Virion . Nucleocapsid protein p7: Virion . Reverse transcriptase/ribonuclease H: Virion . Integrase: Virion : P04585 P04585
• Total number of polymer chains: 2
• Total formula weight: 116778.57

Authors

Lansdon, E.B. (deposition date: 2010-03-31, release date: 2010-05-12, Last modification date: 2023-09-06)

Primary citation

Lansdon, E.B.,Brendza, K.M.,Hung, M.,Wang, R.,Mukund, S.,Jin, D.,Birkus, G.,Kutty, N.,Liu, X.
Crystal Structures of HIV-1 Reverse Transcriptase with Etravirine (TMC125) and Rilpivirine (TMC278): Implications for Drug Design.
J.Med.Chem., 53:4295-4299, 2010

PubMed 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.

PubMed: 20438081
DOI: 10.1021/jm1002233

Experimental method

X-RAY DIFFRACTION (2.8 Å)