3EYM

Structure of Influenza Haemagglutinin in complex with an inhibitor of membrane fusion

3EYM の概要

• エントリーDOI: 10.2210/pdb3eym/pdb
• 関連するPDBエントリー: 3EYJ 3EYM
• 分子名称: Hemagglutinin HA1 chain, Hemagglutinin HA2 chain, 2-tert-butylbenzene-1,4-diol (3 entities in total)
• 機能のキーワード: influenza, hemagglutinin, inhibitor, envelope protein, fusion protein, glycoprotein, lipoprotein, membrane, palmitate, transmembrane, virion, viral protein
• 由来する生物種: Influenza A virus; 詳細
• 細胞内の位置: Virion membrane; Single-pass type I membrane protein (Potential): P03437 P03437
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 166344.00

構造登録者

Russell, R.J.,Kerry, P.S.,Stevens, D.A.,Steinhauer, D.A.,Martin, S.R.,Gamblin, S.J.,Skehel, J.J. (登録日: 2008-10-21, 公開日: 2009-01-13, 最終更新日: 2024-11-20)

主引用文献

Russell, R.J.,Kerry, P.S.,Stevens, D.J.,Steinhauer, D.A.,Martin, S.R.,Gamblin, S.J.,Skehel, J.J.
Structure of influenza hemagglutinin in complex with an inhibitor of membrane fusion
Proc.Natl.Acad.Sci.USA, 105:17736-17741, 2008

PubMed Abstract: The influenza surface glycoprotein hemagglutinin (HA) is a potential target for antiviral drugs because of its key roles in the initial stages of infection: receptor binding and the fusion of virus and cell membranes. The structure of HA in complex with a known inhibitor of membrane fusion and virus infectivity, tert-butyl hydroquinone (TBHQ), shows that the inhibitor binds in a hydrophobic pocket formed at an interface between HA monomers. Occupation of this site by TBHQ stabilizes the neutral pH structure through intersubunit and intrasubunit interactions that presumably inhibit the conformational rearrangements required for membrane fusion. The nature of the binding site suggests routes for the chemical modification of TBHQ that could lead to the development of more potent inhibitors of membrane fusion and potential anti-influenza drugs.

PubMed: 19004788
DOI: 10.1073/pnas.0807142105

実験手法

X-RAY DIFFRACTION (2.8 Å)