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-Structure paper
Title | The structure of native influenza virion ribonucleoproteins. |
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Journal, issue, pages | Science, Vol. 338, Issue 6114, Page 1634-1637, Year 2012 |
Publish date | Dec 21, 2012 |
Authors | Rocío Arranz / Rocío Coloma / Francisco Javier Chichón / José Javier Conesa / José L Carrascosa / José M Valpuesta / Juan Ortín / Jaime Martín-Benito / |
PubMed Abstract | The influenza viruses cause annual epidemics of respiratory disease and occasional pandemics, which constitute a major public-health issue. The segmented negative-stranded RNAs are associated with ...The influenza viruses cause annual epidemics of respiratory disease and occasional pandemics, which constitute a major public-health issue. The segmented negative-stranded RNAs are associated with the polymerase complex and nucleoprotein (NP), forming ribonucleoproteins (RNPs), which are responsible for virus transcription and replication. We describe the structure of native RNPs derived from virions. They show a double-helical conformation in which two NP strands of opposite polarity are associated with each other along the helix. Both strands are connected by a short loop at one end of the particle and interact with the polymerase complex at the other end. This structure will be relevant for unraveling the mechanisms of nuclear import of parental virus RNPs, their transcription and replication, and the encapsidation of progeny RNPs into virions. |
External links | Science / PubMed:23180776 |
Methods | EM (helical sym.) / EM (single particle) |
Resolution | 18.0 - 27.0 Å |
Structure data | EMDB-2205, PDB-4bbl: EMDB-2206: EMDB-2207: EMDB-2208: |
Source |
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Keywords | NUCLEAR PROTEIN / NUCLEOCAPSID |