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5INE

Crystal structure of the prefusion glycoprotein of LCMV

5INE の概要
エントリーDOI10.2210/pdb5ine/pdb
分子名称Pre-glycoprotein polyprotein GP complex, alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
機能のキーワードarenavirus, lcmv, glycoprotein, pre-fusion, viral protein
由来する生物種Lymphocytic choriomeningitis mammarenavirus
タンパク質・核酸の鎖数2
化学式量合計107866.16
構造登録者
Hastie, K.M.,Saphire, E.O. (登録日: 2016-03-07, 公開日: 2016-04-20, 最終更新日: 2024-10-23)
主引用文献Hastie, K.M.,Igonet, S.,Sullivan, B.M.,Legrand, P.,Zandonatti, M.A.,Robinson, J.E.,Garry, R.F.,Rey, F.A.,Oldstone, M.B.,Saphire, E.O.
Crystal structure of the prefusion surface glycoprotein of the prototypic arenavirus LCMV.
Nat.Struct.Mol.Biol., 23:513-521, 2016
Cited by
PubMed Abstract: Arenaviruses exist worldwide and can cause hemorrhagic fever and neurologic disease. A single glycoprotein expressed on the viral surface mediates entry into target cells. This glycoprotein, termed GPC, contains a membrane-associated signal peptide, a receptor-binding subunit termed GP1 and a fusion-mediating subunit termed GP2. Although GPC is a critical target of antibodies and vaccines, the structure of the metastable GP1-GP2 prefusion complex has remained elusive for all arenaviruses. Here we describe the crystal structure of the fully glycosylated prefusion GP1-GP2 complex of the prototypic arenavirus LCMV at 3.5 Å. This structure reveals the conformational changes that the arenavirus glycoprotein must undergo to cause fusion and illustrates the fusion regions and potential oligomeric states.
PubMed: 27111888
DOI: 10.1038/nsmb.3210
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3.5 Å)
構造検証レポート
Validation report summary of 5ine
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2024-10-30に公開中

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