9KNT

ERDRP-0519-bound measles virus L-P complex

これはPDB形式変換不可エントリーです。

9KNT の概要

• エントリーDOI: 10.2210/pdb9knt/pdb
• EMDBエントリー: 62459 62461
• 分子名称: RNA-directed RNA polymerase L, Phosphoprotein, ZINC ION, ... (4 entities in total)
• 機能のキーワード: complex, transcription
• 由来する生物種: Measles virus strain Ichinose-B95a; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 410600.69

構造登録者

Wang, Y.R.,Zhang, H.Q. (登録日: 2024-11-19, 公開日: 2025-07-16, 最終更新日: 2025-09-24)

主引用文献

Wang, Y.,Zhao, L.,Zhang, Y.,Gao, X.,Wang, Y.,Shi, W.,Kornberg, R.D.,Zhang, H.
Structures of the measles virus polymerase complex with non-nucleoside inhibitors and mechanism of inhibition.
Cell, 188:4913-, 2025

PubMed Abstract: The measles virus (MeV), a highly contagious non-segmented negative-sense RNA virus in the Paramyxoviridae family, causes millions of infections annually, with no approved antivirals available. The viral polymerase complex, comprising the large (L) protein and the tetrameric phosphoprotein (P), is a key antiviral target. We determined the cryo-electron microscopy structures of the MeV polymerase complex alone and bound to two non-nucleoside inhibitors, ERDRP-0519 and AS-136A. Inhibitor binding induces a conformational change in the catalytic loop, allosterically locking the polymerase in an inactive "GDN-out" state. These findings led to the proposal that ERDRP-0519 would also be effective against Nipah virus (NiV), a highly pathogenic virus with no available antivirals. This proposal was confirmed by structure determination of the NiV polymerase complex and by inhibition of transcription.

PubMed: 40628260
DOI: 10.1016/j.cell.2025.06.017

実験手法

ELECTRON MICROSCOPY (3.4 Å)