Summary information and primary citation
- PDB-id
- 4uft; SNAP-derived features in text and JSON formats;
DNAproDB
- Class
- RNA binding protein
- Method
- cryo-EM (4.3 Å)
- Summary
- Structure of the helical measles virus nucleocapsid
- Reference
- Gutsche I, Desfosses A, Effantin G, Ling WL, Haupt M, Ruigrok RWH, Sachse C, Schoehn G (2015): "Near-Atomic Cryo-Em Structure of the Helical Measles Virus Nucleocapsid." Science, 348, 704. doi: 10.1126/SCIENCE.AAA5137.
- Abstract
- Measles is a highly contagious human disease. We used cryo-electron microscopy and single particle-based helical image analysis to determine the 4.3 Å resolution structure of the helical nucleocapsid formed by the folded domain of the Measles Virus nucleoprotein encapsidating an RNA. The resulting pseudoatomic model of the Measles Virus nucleocapsid offers important insights into the mechanism of the helical polymerisation of nucleocapsids of negative-strand RNA viruses, in particular via the exchange subdomains of the nucleoprotein.The structure reveals the mode of the nucleoprotein-RNA interaction and explains why each nucleoprotein of Measles Virus binds six nucleotides whereas the Respiratory Syncytial Virus nucleoprotein binds seven. It provides a rational basis for further analysis of Measles Virus replication and transcription, and reveals potential targets for drug design.
