6BKO

Crystal structure of the A/Wyoming/3/2003 (H3N2) influenza virus hemagglutinin D190E mutant apo form

6BKO の概要

• エントリーDOI: 10.2210/pdb6bko/pdb
• 分子名称: Hemagglutinin, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 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, ... (7 entities in total)
• 機能のキーワード: influenza, hemagglutinin, receptor, viral protein
• 由来する生物種: Influenza A virus (A/Wyoming/3e/2003(H3)); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 59159.71

構造登録者

Wu, N.C.,Wilson, I.A. (登録日: 2017-11-09, 公開日: 2018-02-28, 最終更新日: 2023-10-04)

主引用文献

Wu, N.C.,Thompson, A.J.,Xie, J.,Lin, C.W.,Nycholat, C.M.,Zhu, X.,Lerner, R.A.,Paulson, J.C.,Wilson, I.A.
A complex epistatic network limits the mutational reversibility in the influenza hemagglutinin receptor-binding site.
Nat Commun, 9:1264-1264, 2018

PubMed Abstract: The hemagglutinin (HA) receptor-binding site (RBS) in human influenza A viruses is critical for attachment to host cells, which imposes a functional constraint on its natural evolution. On the other hand, being part of the major antigenic sites, the HA RBS of human H3N2 viruses needs to constantly mutate to evade the immune system. From large-scale mutagenesis experiments, we here show that several of the natural RBS substitutions become integrated into an extensive epistatic network that prevents substitution reversion. X-ray structural analysis reveals the mechanistic consequences as well as changes in the mode of receptor binding. Further studies are necessary to elucidate whether such entrenchment limits future options for immune escape or adversely affect long-term viral fitness.

PubMed: 29593268
DOI: 10.1038/s41467-018-03663-5

実験手法

X-RAY DIFFRACTION (1.85 Å)