8P24
The crystal structure of the C-terminal domain of Mengla nucleoprotein
Summary for 8P24
| Entry DOI | 10.2210/pdb8p24/pdb |
| Descriptor | Nucleoprotein (1 entity in total) |
| Functional Keywords | nucleoprotein, viral protein, filovirus, mengla |
| Biological source | Mengla dianlovirus |
| Total number of polymer chains | 28 |
| Total formula weight | 399771.15 |
| Authors | Ferrero, D.S.,Tomas Gilabert, O.,Verdaguer, N. (deposition date: 2023-05-14, release date: 2023-10-18, Last modification date: 2023-12-27) |
| Primary citation | Ferrero, D.S.,Tomas Gilabert, O.,Verdaguer, N. Structural insights on the nucleoprotein C-terminal domain of Mengla virus. Microbiol Spectr, 11:e0237323-e0237323, 2023 Cited by PubMed Abstract: Filoviruses are the causative agents of severe and often fatal hemorrhagic disease in humans. Měnglà virus (MLAV) is a recently reported filovirus, isolated from fruit bats that is capable to replicate in human cells, representing a potential risk for human health. An in-depth structural and functional knowledge of MLAV proteins is an essential step for antiviral research on this virus that can also be extended to other emerging filoviruses. In this study, we determined the first crystal structures of the C-terminal domain (CTD) of the MLAV nucleoprotein (NP), showing important similarities to the equivalent domain in MARV. The structural data also show that the NP CTD has the ability to form large helical oligomers that may participate in the control of cytoplasmic inclusion body formation during viral replication. PubMed: 37888996DOI: 10.1128/spectrum.02373-23 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.73 Å) |
Structure validation
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