2X5I
Crystal structure echovirus 7
2X5I の概要
| エントリーDOI | 10.2210/pdb2x5i/pdb |
| 分子名称 | VP1, VP2, VP3, ... (5 entities in total) |
| 機能のキーワード | virus, capsid protein |
| 由来する生物種 | HUMAN ECHOVIRUS 7 詳細 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 96412.65 |
| 構造登録者 | Plevka, P.,Hafenstein, S.,Zhang, Y.,Bowman, V.D.,Chipman, P.R.,Bator, C.M.,Rossmann, M.G. (登録日: 2010-02-08, 公開日: 2010-12-22, 最終更新日: 2023-12-20) |
| 主引用文献 | Plevka, P.,Hafenstein, S.,Harris, K.G.,Cifuente, J.O.,Zhang, Y.,Bowman, V.D.,Chipman, P.R.,Bator, C.M.,Lin, F.,Medof, M.E.,Rossmann, M.G. Interaction of Decay-Accelerating Factor with Echovirus 7. J.Virol., 84:12665-, 2010 Cited by PubMed Abstract: Echovirus 7 (EV7) belongs to the Enterovirus genus within the family Picornaviridae. Many picornaviruses use IgG-like receptors that bind in the viral canyon and are required to initiate viral uncoating during infection. However, in addition, some of the enteroviruses use an alternative or additional receptor that binds outside the canyon. Decay-accelerating factor (DAF) has been identified as a cellular receptor for EV7. The crystal structure of EV7 has been determined to 3.1-Å resolution and used to interpret the 7.2-Å-resolution cryo-electron microscopy reconstruction of EV7 complexed with DAF. Each DAF binding site on EV7 is near a 2-fold icosahedral symmetry axis, which differs from the binding site of DAF on the surface of coxsackievirus B3, indicating that there are independent evolutionary processes by which DAF was selected as a picornavirus accessory receptor. This suggests that there is an advantage for these viruses to recognize DAF during the initial process of infection. PubMed: 20881044DOI: 10.1128/JVI.00837-10 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.1 Å) |
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