6XYE
Cryo-EM structure of the prefusion state of canine distemper virus fusion protein ectodomain
6XYE の概要
| エントリーDOI | 10.2210/pdb6xye/pdb |
| EMDBエントリー | 10649 |
| 分子名称 | Fusion glycoprotein F2, Fusion glycoprotein F1 (2 entities in total) |
| 機能のキーワード | fusion protein, prefusion state, viral protein |
| 由来する生物種 | Canine morbillivirus 詳細 |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 172921.25 |
| 構造登録者 | |
| 主引用文献 | Kalbermatter, D.,Shrestha, N.,Gall, F.M.,Wyss, M.,Riedl, R.,Plattet, P.,Fotiadis, D. Cryo-EM structure of the prefusion state of canine distemper virus fusion protein ectodomain. J Struct Biol X, 4:100021-100021, 2020 Cited by PubMed Abstract: Measles virus (MeV) and canine distemper virus (CDV), two members of the genus, are still causing important global diseases of humans and animals, respectively. To enter target cells, morbilliviruses rely on an envelope-anchored machinery, which is composed of two interacting glycoproteins: a tetrameric receptor binding (H) protein and a trimeric fusion (F) protein. To execute membrane fusion, the F protein initially adopts a metastable, prefusion state that refolds into a highly stable postfusion conformation as the result of a finely coordinated activation process mediated by the H protein. Here, we employed cryo-electron microscopy (cryo-EM) and single particle reconstruction to elucidate the structure of the prefusion state of the CDV F protein ectodomain (solF) at 4.3 Å resolution. Stabilization of the prefusion solF trimer was achieved by fusing the GCNt trimerization sequence at the C-terminal protein region, and expressing and purifying the recombinant protein in the presence of a morbilliviral fusion inhibitor class compound. The three-dimensional cryo-EM map of prefusion CDV solF in complex with the inhibitor clearly shows density for the ligand at the protein binding site suggesting common mechanisms of membrane fusion activation and inhibition employed by different morbillivirus members. PubMed: 32647825DOI: 10.1016/j.yjsbx.2020.100021 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (4.3 Å) |
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