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4O6D

West Nile Virus Non-structural protein 1 (NS1) Form 1 crystal

4O6D の概要
エントリーDOI10.2210/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
Akey, D.L.,Smith, J.L. (登録日: 2013-12-20, 公開日: 2014-02-19, 最終更新日: 2024-11-06)
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: 24505133
DOI: 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)
構造検証レポート
Validation report summary of 4o6d
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-11-06に公開中

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