1H2C
Ebola virus matrix protein VP40 N-terminal domain in complex with RNA (High-resolution VP40[55-194] variant).
1H2C の概要
エントリーDOI | 10.2210/pdb1h2c/pdb |
関連するPDBエントリー | 1H2D |
分子名称 | MATRIX PROTEIN VP40, 5'-R(*UP*GP*AP)-3' (3 entities in total) |
機能のキーワード | virus/viral protein, filovirus, ebola virus, matrix protein vp40, assembly, budding, virus-viral protein complex |
由来する生物種 | EBOLA VIRUS 詳細 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 16258.25 |
構造登録者 | Gomis-Ruth, F.X.,Dessen, A.,Bracher, A.,Klenk, H.D.,Weissenhorn, W. (登録日: 2002-08-05, 公開日: 2003-04-10, 最終更新日: 2024-05-08) |
主引用文献 | Gomis-Ruth, F.X.,Dessen, A.,Timmins, J.,Bracher, A.,Kolesnikowa, L.,Becker, S.,Klenk, H.D.,Weissenhorn, W. The Matrix Protein Vp40 from Ebola Virus Octamerizes Into Pore-Like Structures with Specific RNA Binding Properties Structure, 11:423-, 2003 Cited by PubMed Abstract: The Ebola virus membrane-associated matrix protein VP40 is thought to be crucial for assembly and budding of virus particles. Here we present the crystal structure of a disk-shaped octameric form of VP40 formed by four antiparallel homodimers of the N-terminal domain. The octamer binds an RNA triribonucleotide containing the sequence 5'-U-G-A-3' through its inner pore surface, and its oligomerization and RNA binding properties are facilitated by two conformational changes when compared to monomeric VP40. The selective RNA interaction stabilizes the ring structure and confers in vitro SDS resistance to octameric VP40. SDS-resistant octameric VP40 is also found in Ebola virus-infected cells, which suggests that VP40 has an additional function in the life cycle of the virus besides promoting virus assembly and budding off the plasma membrane. PubMed: 12679020DOI: 10.1016/S0969-2126(03)00050-9 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.6 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード
