9C4H

Double helical structure of influenza D RNP complex

9C4H の概要

• エントリーDOI: 10.2210/pdb9c4h/pdb
• EMDBエントリー: 44980
• 分子名称: Nucleoprotein, viral RNA (2 entities in total)
• 機能のキーワード: influenza, ribonucleoprotein complex, nucleoprotein, viral protein, rna binding protein-rna complex, rna binding protein/rna
• 由来する生物種: Influenza D virus; 詳細
• タンパク質・核酸の鎖数: 17
• 化学式量合計: 1246977.23

構造登録者

Peng, R.,Chang, Y.-W. (登録日: 2024-06-04, 公開日: 2025-05-14, 最終更新日: 2025-05-28)

主引用文献

Peng, R.,Xu, X.,Nepal, B.,Gong, Y.,Li, F.,Ferretti, M.B.,Zhou, M.,Lynch, K.W.,Burslem, G.M.,Kortagere, S.,Marmorstein, R.,Chang, Y.W.
Molecular basis of influenza ribonucleoprotein complex assembly and processive RNA synthesis.
Science, 388:eadq7597-eadq7597, 2025

PubMed Abstract: Influenza viruses replicate and transcribe their genome in the context of a conserved ribonucleoprotein (RNP) complex. By integrating cryo-electron microscopy single-particle analysis and cryo-electron tomography, we define the influenza RNP as a right-handed, antiparallel double helix with the viral RNA encapsidated in the minor groove. Individual nucleoprotein subunits are connected by a flexible tail loop that inserts into a conserved pocket in its neighbor. We visualize the viral polymerase in RNP at different functional states, revealing how it accesses the RNA template while maintaining the double-helical architecture of RNP by strand sliding. Targeting the tail loop binding interface, we identify lead compounds as potential anti-influenza inhibitors. These findings elucidate the molecular determinants underpinning influenza virus replication and highlight a promising target for antiviral development.

PubMed: 40373132
DOI: 10.1126/science.adq7597

実験手法

ELECTRON MICROSCOPY (8.6 Å)