1TG8
The structure of Dengue virus E glycoprotein
1TG8 の概要
| エントリーDOI | 10.2210/pdb1tg8/pdb |
| 関連するPDBエントリー | 1TGE 1THD |
| 分子名称 | envelope glycoprotein, 2-acetamido-2-deoxy-alpha-D-glucopyranose (3 entities in total) |
| 機能のキーワード | flavivirus e conformation, viral protein |
| 由来する生物種 | Dengue virus 2 |
| 細胞内の位置 | Envelope protein E: Virion membrane; Multi- pass membrane protein (By similarity). Non-structural protein 1: Secreted. Non-structural protein 2A-alpha: Host endoplasmic reticulum membrane; Multi-pass membrane protein (Potential). Non-structural protein 2A: Host endoplasmic reticulum membrane; Multi-pass membrane protein (Potential). Serine protease NS3: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): P27914 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 44305.81 |
| 構造登録者 | Zhang, Y.,Zhang, W.,Ogata, S.,Clements, D.,Strauss, J.H.,Baker, T.S.,Rossmann, M.G. (登録日: 2004-05-28, 公開日: 2004-09-28, 最終更新日: 2024-11-13) |
| 主引用文献 | Zhang, Y.,Zhang, W.,Ogata, S.,Clements, D.,Strauss, J.H.,Baker, T.S.,Kuhn, R.J.,Rossmann, M.G. Conformational changes of the flavivirus e glycoprotein Structure, 12:1607-1618, 2004 Cited by PubMed Abstract: Dengue virus, a member of the Flaviviridae family, has a surface composed of 180 copies each of the envelope (E) glycoprotein and the membrane (M) protein. The crystal structure of an N-terminal fragment of E has been determined and compared with a previously described structure. The primary difference between these structures is a 10 degrees rotation about a hinge relating the fusion domain DII to domains DI and DIII. These two rigid body components were used for independent fitting of E into the cryo-electron microscopy maps of both immature and mature dengue viruses. The fitted E structures in these two particles showed a difference of 27 degrees between the two components. Comparison of the E structure in its postfusion state with that in the immature and mature virions shows a rotation approximately around the same hinge. Flexibility of E is apparently a functional requirement for assembly and infection of flaviviruses. PubMed: 15341726DOI: 10.1016/j.str.2004.06.019 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.61 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






