3MED

HIV-1 K103N Reverse Transcriptase in Complex with TMC125

3MED の概要

• エントリーDOI: 10.2210/pdb3med/pdb
• 関連するPDBエントリー: 3MEC 3MEE 3MEG
• 分子名称: p66 Reverse transcriptase, p51 Reverse transcriptase, 4-({6-AMINO-5-BROMO-2-[(4-CYANOPHENYL)AMINO]PYRIMIDIN-4-YL}OXY)-3,5-DIMETHYLBENZONITRILE, ... (6 entities in total)
• 機能のキーワード: hiv, reverse transcriptase, tmc125, etravirine, nnrti, transferase
• 由来する生物種: HIV-1 M:B_HXB2R (HIV-1); 詳細
• 細胞内の位置: Matrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential). Reverse transcriptase/ribonuclease H: Virion (Potential). Integrase: Virion (Potential): P04585 P04585
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 116978.95

構造登録者

Lansdon, E.B. (登録日: 2010-03-31, 公開日: 2010-05-12, 最終更新日: 2023-09-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.5 Å)