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 structure of the helical nucleocapsid formed by the folded domain of the measles virus nucleoprotein encapsidating an RNA at a resolution of 4.3 angstroms. The resulting pseudoatomic model of the measles virus nucleocapsid offers important insights into the mechanism of the helical polymerization 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.
