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6LGX

Structure of Rabies virus glycoprotein at basic pH

6LGX の概要
エントリーDOI10.2210/pdb6lgx/pdb
分子名称Glycoprotein,Glycoprotein,Glycoprotein (1 entity in total)
機能のキーワードfunctional class, viral protein
由来する生物種Rabies lyssavirus
詳細
タンパク質・核酸の鎖数2
化学式量合計99266.56
構造登録者
主引用文献Yang, F.,Lin, S.,Ye, F.,Yang, J.,Qi, J.,Chen, Z.,Lin, X.,Wang, J.,Yue, D.,Cheng, Y.,Chen, Z.,Chen, H.,You, Y.,Zhang, Z.,Yang, Y.,Yang, M.,Sun, H.,Li, Y.,Cao, Y.,Yang, S.,Wei, Y.,Gao, G.F.,Lu, G.
Structural Analysis of Rabies Virus Glycoprotein Reveals pH-Dependent Conformational Changes and Interactions with a Neutralizing Antibody.
Cell Host Microbe, 27:441-, 2020
Cited by
PubMed Abstract: Rabies virus (RABV), the etiological agent for the lethal disease of rabies, is a deadly zoonotic pathogen. The RABV glycoprotein (RABV-G) is a key factor mediating virus entry and the major target of neutralizing antibodies. Here, we report the crystal structures of RABV-G solved in the free form at ∼pH-8.0 and in the complex form with a neutralizing antibody 523-11 at ∼pH-6.5, respectively. RABV-G has three domains, and the basic-to-acidic pH change results in large domain re-orientations and concomitant domain-linker re-constructions, switching it from a bent hairpin conformation into an extended conformation. During such low-pH-induced structural transitions, residues located in the domain-linker are found to play important roles in glycoprotein-mediated membrane fusion. Finally, the antibody interacts with RABV-G mainly through its heavy chain and binds to a bipartite conformational epitope in the viral protein for neutralization. These structures provide valuable information for vaccine and drug design.
PubMed: 32004500
DOI: 10.1016/j.chom.2019.12.012
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3.097 Å)
構造検証レポート
Validation report summary of 6lgx
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2026-04-29に公開中

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