2GTT
Crystal structure of the rabies virus nucleoprotein-RNA complex
2GTT の概要
| エントリーDOI | 10.2210/pdb2gtt/pdb |
| 分子名称 | Nucleoprotein, RNA (99-MER), PHOSPHATE ION, ... (4 entities in total) |
| 機能のキーワード | protein-rna complex, rabies virus, nucleoprotein, viral protein, rna binding protein |
| 由来する生物種 | Lyssavirus rabies 詳細 |
| タンパク質・核酸の鎖数 | 24 |
| 化学式量合計 | 1176436.18 |
| 構造登録者 | Albertini, A.A.V.,Wernimont, A.K.,Muziol, T.,Ravelli, R.B.G.,Weissenhorn, W.,Ruigrok, R.W.H. (登録日: 2006-04-28, 公開日: 2006-09-19, 最終更新日: 2023-10-18) |
| 主引用文献 | Albertini, A.A.V.,Wernimont, A.K.,Muziol, T.,Ravelli, R.B.G.,Clapier, C.R.,Schoehn, G.,Weissenhorn, W.,Ruigrok, R.W.H. Crystal Structure of the Rabies Virus Nucleoprotein-RNA Complex Science, 313:360-363, 2006 Cited by PubMed Abstract: Negative-strand RNA viruses condense their genome into a helical nucleoprotein-RNA complex, the nucleocapsid, which is packed into virions and serves as a template for the RNA-dependent RNA polymerase complex. The crystal structure of a recombinant rabies virus nucleoprotein-RNA complex, organized in an undecameric ring, has been determined at 3.5 angstrom resolution. Polymerization of the nucleoprotein is achieved by domain exchange between protomers, with flexible hinges allowing nucleocapsid formation. The two core domains of the nucleoprotein clamp around the RNA at their interface and shield it from the environment. RNA sequestering by nucleoproteins is likely a common mechanism used by negative-strand RNA viruses to protect their genomes from the innate immune response directed against viral RNA in human host cells at certain stages of an infectious cycle. PubMed: 16778023DOI: 10.1126/science.1125280 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.49 Å) |
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