4ILD
Crystal structure of truncated Bovine viral diarrhea virus 1 E2 envelope protein
4ILD の概要
| エントリーDOI | 10.2210/pdb4ild/pdb |
| 分子名称 | Envelope glycoprotein E2, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (4 entities in total) |
| 機能のキーワード | bvdv1, viral envelope protein, viral membrane fusion, e1 envelope protein, viral surface membrane, viral protein |
| 由来する生物種 | Bovine viral diarrhea virus 1-NADL (BVDV) |
| 細胞内の位置 | E(rns) glycoprotein: Host membrane; Peripheral membrane protein. Envelope glycoprotein E2: Host cell surface. Cysteine protease NS2: Host membrane; Multi- pass membrane protein (Potential): P19711 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 62069.15 |
| 構造登録者 | |
| 主引用文献 | Li, Y.,Wang, J.,Kanai, R.,Modis, Y. Crystal structure of glycoprotein E2 from bovine viral diarrhea virus. Proc.Natl.Acad.Sci.USA, 110:6805-6810, 2013 Cited by PubMed Abstract: Pestiviruses, including bovine viral diarrhea virus, are important animal pathogens and are closely related to hepatitis C virus, which remains a major global health threat. They have an outer lipid envelope bearing two glycoproteins, E1 and E2, required for cell entry. They deliver their genome into the host cell cytoplasm by fusion of their envelope with a cellular membrane. The crystal structure of bovine viral diarrhea virus E2 reveals a unique protein architecture consisting of two Ig-like domains followed by an elongated β-stranded domain with a new fold. E2 forms end-to-end homodimers with a conserved C-terminal motif rich in aromatic residues at the contact. A disulfide bond across the interface explains the acid resistance of pestiviruses and their requirement for a redox activation step to initiate fusion. From the structure of E2, we propose alternative possible membrane fusion mechanisms. We expect the pestivirus fusion apparatus to be conserved in hepatitis C virus. PubMed: 23569276DOI: 10.1073/pnas.1300524110 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.27 Å) |
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