4O6D
West Nile Virus Non-structural protein 1 (NS1) Form 1 crystal
4O6D の概要
エントリーDOI | 10.2210/pdb4o6d/pdb |
関連するPDBエントリー | 4O6B 4O6C |
分子名称 | NS1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total) |
機能のキーワード | flavivirus, non-structural protein 1, ns1, viral protein |
由来する生物種 | West Nile virus (WNV) 詳細 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 90167.90 |
構造登録者 | |
主引用文献 | Akey, D.L.,Brown, W.C.,Dutta, S.,Konwerski, J.,Jose, J.,Jurkiw, T.J.,DelProposto, J.,Ogata, C.M.,Skiniotis, G.,Kuhn, R.J.,Smith, J.L. Flavivirus NS1 structures reveal surfaces for associations with membranes and the immune system. Science, 343:881-885, 2014 Cited by PubMed Abstract: Flaviviruses, the human pathogens responsible for dengue fever, West Nile fever, tick-borne encephalitis, and yellow fever, are endemic in tropical and temperate parts of the world. The flavivirus nonstructural protein 1 (NS1) functions in genome replication as an intracellular dimer and in immune system evasion as a secreted hexamer. We report crystal structures for full-length, glycosylated NS1 from West Nile and dengue viruses. The NS1 hexamer in crystal structures is similar to a solution hexamer visualized by single-particle electron microscopy. Recombinant NS1 binds to lipid bilayers and remodels large liposomes into lipoprotein nanoparticles. The NS1 structures reveal distinct domains for membrane association of the dimer and interactions with the immune system and are a basis for elucidating the molecular mechanism of NS1 function. PubMed: 24505133DOI: 10.1126/science.1247749 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.5936 Å) |
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