4WE5

The crystal structure of hemagglutinin from A/Port Chalmers/1/1973 influenza virus

4WE5 の概要

• エントリーDOI: 10.2210/pdb4we5/pdb
• 関連するPDBエントリー: 4WE4 4WE6 4WE7 4WE8 4WE9 4WEA
• 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: hemagglutinin, h3n2, influenza virus, 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 : Q1PUD9 Q1PUD9
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 59006.57

構造登録者

Yang, H.,Carney, P.J.,Chang, J.C.,Guo, Z.,Villanueva, J.M.,Stevens, J. (登録日: 2014-09-09, 公開日: 2015-02-11, 最終更新日: 2024-10-23)

主引用文献

Yang, H.,Carney, P.J.,Chang, J.C.,Guo, Z.,Villanueva, J.M.,Stevens, J.
Structure and receptor binding preferences of recombinant human A(H3N2) virus hemagglutinins.
Virology, 477C:18-31, 2015

PubMed Abstract: A(H3N2) influenza viruses have circulated in humans since 1968, and antigenic drift of the hemagglutinin (HA) protein continues to be a driving force that allows the virus to escape the human immune response. Since the major antigenic sites of the HA overlap into the receptor binding site (RBS) of the molecule, the virus constantly struggles to effectively adapt to host immune responses, without compromising its functionality. Here, we have structurally assessed the evolution of the A(H3N2) virus HA RBS, using an established recombinant expression system. Glycan binding specificities of nineteen A(H3N2) influenza virus HAs, each a component of the seasonal influenza vaccine between 1968 and 2012, were analyzed. Results suggest that while its receptor-binding site has evolved from one that can bind a broad range of human receptor analogs to one with a more restricted binding profile for longer glycans, the virus continues to circulate and transmit efficiently among humans.

PubMed: 25617824
DOI: 10.1016/j.virol.2014.12.024

実験手法

X-RAY DIFFRACTION (2.1 Å)