7LRM

Structure of HIV-1 Reverse Transcriptase in complex with DNA, dCTP, and CA(2+) ion

7LRM の概要

• エントリーDOI: 10.2210/pdb7lrm/pdb
• 分子名称: Reverse transcriptase p66, Reverse transcriptase p51, DNA/RNA (38-MER), ... (9 entities in total)
• 機能のキーワード: human immunodeficiency virus 1, protein/dsdna, aptamer, dntp, transferase, transferase-dna complex, transferase/dna
• 由来する生物種: Human immunodeficiency virus type 1 (HIV-1); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 254466.71

構造登録者

Hoang, A.,Ruiz, F.X.,Arnold, E. (登録日: 2021-02-16, 公開日: 2022-02-23, 最終更新日: 2023-10-18)

主引用文献

Ruiz, F.X.,Hoang, A.,Dilmore, C.R.,DeStefano, J.J.,Arnold, E.
Structural basis of HIV inhibition by L-nucleosides: Opportunities for drug development and repurposing.
Drug Discov Today, 27:1832-1846, 2022

PubMed Abstract: Infection with HIV can cripple the immune system and lead to AIDS. Hepatitis B virus (HBV) is a hepadnavirus that causes human liver diseases. Both pathogens are major public health problems affecting millions of people worldwide. The polymerases from both viruses are the most common drug target for viral inhibition, sharing common architecture at their active sites. The L-nucleoside drugs emtricitabine and lamivudine are widely used HIV reverse transcriptase (RT) and HBV polymerase (Pol) inhibitors. Nevertheless, structural details of their binding to RT(Pol)/nucleic acid remained unknown until recently. Here, we discuss the implications of these structures, alongside related complexes with L-dNTPs, for the development of novel L-nucleos(t)ide drugs, and prospects for repurposing them.

PubMed: 35218925
DOI: 10.1016/j.drudis.2022.02.016

実験手法

X-RAY DIFFRACTION (3.14 Å)