3PHE

HCV NS5B with a bound quinolone inhibitor

3PHE の概要

• エントリーDOI: 10.2210/pdb3phe/pdb
• 分子名称: HCV encoded nonstructural 5B protein, 4-chlorobenzyl 6-fluoro-7-(4-methylpiperazin-1-yl)-1-[4-(methylsulfonyl)benzyl]-4-oxo-1,4-dihydroquinoline-3-carboxylate (3 entities in total)
• 機能のキーワード: transferase, polymerase, rna, mitochondrial membrane, transferase-transferase inhibitor complex, transferase/transferase inhibitor
• 由来する生物種: Hepatitis C virus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 258806.20

構造登録者

Somoza, J.R.,To, N.,Lehoux, I. (登録日: 2010-11-03, 公開日: 2010-11-17, 最終更新日: 2024-02-21)

主引用文献

Kumar, D.V.,Rai, R.,Brameld, K.A.,Somoza, J.R.,Rajagopalan, R.,Janc, J.W.,Xia, Y.M.,Ton, T.L.,Shaghafi, M.B.,Hu, H.,Lehoux, I.,To, N.,Young, W.B.,Green, M.J.
Quinolones as HCV NS5B polymerase inhibitors.
Bioorg.Med.Chem.Lett., 21:82-87, 2011

PubMed Abstract: Hepatitis C virus (HCV) infection is treated with a combination of peginterferon alfa-2a/b and ribavirin. To address the limitations of this therapy, numerous small molecule agents are in development, which act by directly affecting key steps in the viral life-cycle. Herein we describe our discovery of quinolone derivatives, novel small-molecules that inhibit NS5b polymerase, a key enzyme of the viral life-cycle. A crystal structure of a quinoline analog bound to NS5B reveals that this class of compounds binds to allosteric site-II (non-nucleoside inhibitor-site 2, NNI-2) of this protein.

PubMed: 21145235
DOI: 10.1016/j.bmcl.2010.11.068

実験手法

X-RAY DIFFRACTION (2.2 Å)