9C4H
Double helical structure of influenza D RNP complex
Summary for 9C4H
| Entry DOI | 10.2210/pdb9c4h/pdb |
| EMDB information | 44980 |
| Descriptor | Nucleoprotein, viral RNA (2 entities in total) |
| Functional Keywords | influenza, ribonucleoprotein complex, nucleoprotein, viral protein, rna binding protein-rna complex, rna binding protein/rna |
| Biological source | Influenza D virus More |
| Total number of polymer chains | 17 |
| Total formula weight | 1246977.23 |
| Authors | Peng, R.,Chang, Y.-W. (deposition date: 2024-06-04, release date: 2025-05-14, Last modification date: 2025-05-28) |
| Primary citation | 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 Cited by 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: 40373132DOI: 10.1126/science.adq7597 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (8.6 Å) |
Structure validation
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