4BBL
Cryo-electron microscopy reconstruction of the helical part of influenza A virus ribonucleoprotein isolated from virions.
4BBL の概要
| エントリーDOI | 10.2210/pdb4bbl/pdb |
| EMDBエントリー | 2205 |
| 分子名称 | NUCLEOPROTEIN, RNA (2 entities in total) |
| 機能のキーワード | nuclear protein, nucleocapsid |
| 由来する生物種 | INFLUENZA A VIRUS 詳細 |
| 細胞内の位置 | Virion : P15682 |
| タンパク質・核酸の鎖数 | 26 |
| 化学式量合計 | 1551852.88 |
| 構造登録者 | Arranz, R.,Coloma, R.,Chichon, F.J.,Conesa, J.J.,Carrascosa, J.L.,Valpuesta, J.M.,Ortin, J.,Martin-Benito, J. (登録日: 2012-09-26, 公開日: 2012-12-05, 最終更新日: 2024-05-08) |
| 主引用文献 | Arranz, R.,Coloma, R.,Chichon, F.J.,Conesa, J.J.,Carrascosa, J.L.,Valpuesta, J.M.,Ortin, J.,Martin-Benito, J. The Structure of Native Influenza Virion Ribonucleoproteins Science, 338:1634-, 2012 Cited by 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 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. PubMed: 23180776DOI: 10.1126/SCIENCE.1228172 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (18 Å) |
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