5N2U
Influenza D virus nucleoprotein
Summary for 5N2U
| Entry DOI | 10.2210/pdb5n2u/pdb |
| Descriptor | Nucleoprotein (2 entities in total) |
| Functional Keywords | influenza virus, nucleoprotein, viral protein |
| Biological source | Influenza D virus (D/bovine/France/2986/2012) |
| Total number of polymer chains | 4 |
| Total formula weight | 245561.44 |
| Authors | Labaronne, A.,Ruigrok, R.W.H.,Crepin, T. (deposition date: 2017-02-08, release date: 2018-02-28, Last modification date: 2024-01-17) |
| Primary citation | Donchet, A.,Oliva, J.,Labaronne, A.,Tengo, L.,Miloudi, M.,C A Gerard, F.,Mas, C.,Schoehn, G.,W H Ruigrok, R.,Ducatez, M.,Crepin, T. The structure of the nucleoprotein of Influenza D shows that all Orthomyxoviridae nucleoproteins have a similar NPCORE, with or without a NPTAILfor nuclear transport. Sci Rep, 9:600-600, 2019 Cited by PubMed Abstract: This paper focuses on the nucleoprotein (NP) of the newly identified member of the Orthomyxoviridae family, Influenza D virus. To date several X-ray structures of NP of Influenza A (A/NP) and B (B/NP) viruses and of infectious salmon anemia (ISA/NP) virus have been solved. Here we purified, characterized and solved the X-ray structure of the tetrameric D/NP at 2.4 Å resolution. The crystal structure of its core is similar to NP of other Influenza viruses. However, unlike A/NP and B/NP which possess a flexible amino-terminal tail containing nuclear localization signals (NLS) for their nuclear import, D/NP possesses a carboxy-terminal tail (D/NP). We show that D/NP harbors a bipartite NLS and designed C-terminal truncated mutants to demonstrate the role of D/NP for nuclear transport. PubMed: 30679709DOI: 10.1038/s41598-018-37306-y PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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