4N5Y

Crystal structure of H5 hemagglutinin mutant (N158D, N224K and Q226L) from the influenza virus A/Viet Nam/1203/2004 (H5N1)

4N5Y の概要

• エントリーDOI: 10.2210/pdb4n5y/pdb
• 関連するPDBエントリー: 2FK0 4N5Z
• 分子名称: Hemagglutinin HA1 chain, Hemagglutinin HA2 chain, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: h5n1, influenza virus, hemagglutinin, viral protein, ferret transmissible
• 由来する生物種: Influenza A virus; 詳細
• タンパク質・核酸の鎖数: 30
• 化学式量合計: 895690.61

構造登録者

Zhu, X.,Wilson, I.A. (登録日: 2013-10-10, 公開日: 2013-11-20, 最終更新日: 2024-10-30)

主引用文献

de Vries, R.P.,Zhu, X.,McBride, R.,Rigter, A.,Hanson, A.,Zhong, G.,Hatta, M.,Xu, R.,Yu, W.,Kawaoka, Y.,de Haan, C.A.,Wilson, I.A.,Paulson, J.C.
Hemagglutinin Receptor Specificity and Structural Analyses of Respiratory Droplet-Transmissible H5N1 Viruses.
J.Virol., 88:768-773, 2014

PubMed Abstract: Two ferret-adapted H5N1 viruses capable of respiratory droplet transmission have been reported with mutations in the hemagglutinin receptor-binding site and stalk domains. Glycan microarray analysis reveals that both viruses exhibit a strong shift toward binding to "human-type" α2-6 sialosides but with notable differences in fine specificity. Crystal structure analysis further shows that the stalk mutation causes no obvious perturbation of the receptor-binding pocket, consistent with its impact on hemagglutinin stability without affecting receptor specificity.

PubMed: 24173215
DOI: 10.1128/JVI.02690-13

実験手法

X-RAY DIFFRACTION (3.1615 Å)