2H0P
NMR Structure of the Dengue-4 virus Envelope Protein Domain III
2H0P の概要
| エントリーDOI | 10.2210/pdb2h0p/pdb |
| NMR情報 | BMRB: 7087 |
| 分子名称 | Envelope glycoprotein (1 entity in total) |
| 機能のキーワード | beta sandwich, ig-fold, viral protein |
| 由来する生物種 | Dengue virus 4 |
| 細胞内の位置 | Envelope protein E: Virion membrane; Multi- pass membrane protein: Q9IZI6 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 12235.13 |
| 構造登録者 | Volk, D.E.,Lee, Y.,Li, X.,Thiviyanathan, V.,Barrett, A.D.T.,Gorenstein, D.G. (登録日: 2006-05-15, 公開日: 2007-03-27, 最終更新日: 2024-11-13) |
| 主引用文献 | Volk, D.E.,Lee, Y.C.,Li, X.,Thiviyanathan, V.,Gromowski, G.D.,Li, L.,Lamb, A.R.,Beasley, D.W.,Barrett, A.D.,Gorenstein, D.G. Solution structure of the envelope protein domain III of dengue-4 virus. Virology, 364:147-154, 2007 Cited by PubMed Abstract: The disease dengue (DEN) is caused by four serologically related viruses termed DEN1, DEN2, DEN3 and DEN4. The structure of the ectodomain of the envelope protein has been determined previously for DEN2 and DEN3 viruses. Using NMR spectroscopic methods, we solved the solution structure of domain III (ED3), the receptor-binding domain, of the envelope protein of DEN4 virus, human strain 703-4. The structure shows that the nine amino acid changes in ED3 that separate the sylvatic and human DEN4 strains are surface exposed. Important structural differences between DEN4-rED3 and ED3 domains of DEN2, DEN3 and other flaviviruses are discussed. PubMed: 17395234DOI: 10.1016/j.virol.2007.02.023 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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