9BDQ
The structure of NiV L-P complex
Summary for 9BDQ
| Entry DOI | 10.2210/pdb9bdq/pdb |
| EMDB information | 44465 |
| Descriptor | RNA-directed RNA polymerase L, Phosphoprotein, ZINC ION (3 entities in total) |
| Functional Keywords | rdrp complex, l-p complex, nipah virus, viral protein |
| Biological source | Henipavirus nipahense More |
| Total number of polymer chains | 5 |
| Total formula weight | 570288.44 |
| Authors | Hu, S.,Yang, P.,Yu, Z.,Abraham, J. (deposition date: 2024-04-12, release date: 2025-01-29, Last modification date: 2025-02-19) |
| Primary citation | Hu, S.,Kim, H.,Yang, P.,Yu, Z.,Ludeke, B.,Mobilia, S.,Pan, J.,Stratton, M.,Bian, Y.,Fearns, R.,Abraham, J. Structural and functional analysis of the Nipah virus polymerase complex. Cell, 188:688-703.e18, 2025 Cited by PubMed Abstract: Nipah virus (NiV) is a bat-borne, zoonotic RNA virus that is highly pathogenic in humans. The NiV polymerase, which mediates viral genome replication and mRNA transcription, is a promising drug target. We determined the cryoelectron microscopy (cryo-EM) structure of the NiV polymerase complex, comprising the large protein (L) and phosphoprotein (P), and performed structural, biophysical, and in-depth functional analyses of the NiV polymerase. The L protein assembles with a long P tetrameric coiled-coil that is capped by a bundle of ⍺-helices that we show are likely dynamic in solution. Docking studies with a known L inhibitor clarify mechanisms of antiviral drug resistance. In addition, we identified L protein features that are required for both transcription and RNA replication and mutations that have a greater impact on RNA replication than on transcription. Our findings have the potential to aid in the rational development of drugs to combat NiV infection. PubMed: 39837328DOI: 10.1016/j.cell.2024.12.021 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.26 Å) |
Structure validation
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