4LXV

Crystal Structure of the Hemagglutinin from a H1N1pdm A/WASHINGTON/5/2011 virus

4LXV の概要

• エントリーDOI: 10.2210/pdb4lxv/pdb
• 分子名称: Hemagglutinin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: hemagglutinin, pandemic, influenza, viral protein
• 由来する生物種: Influenza A virus; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 350147.70

構造登録者

Yang, H.,Chang, J.C.,Guo, Z.,Carney, P.J.,Shore, D.A.,Donis, R.O.,Cox, N.J.,Villanueva, J.M.,Klimov, A.I.,Stevens, J. (登録日: 2013-07-30, 公開日: 2014-02-26, 最終更新日: 2024-10-16)

主引用文献

Yang, H.,Chang, J.C.,Guo, Z.,Carney, P.J.,Shore, D.A.,Donis, R.O.,Cox, N.J.,Villanueva, J.M.,Klimov, A.I.,Stevens, J.
Structural Stability of Influenza A(H1N1)pdm09 Virus Hemagglutinins.
J.Virol., 88:4828-4838, 2014

PubMed Abstract: The noncovalent interactions that mediate trimerization of the influenza hemagglutinin (HA) are important determinants of its biological activities. Recent studies have demonstrated that mutations in the HA trimer interface affect the thermal and pH sensitivities of HA, suggesting a possible impact on vaccine stability (). We used size exclusion chromatography analysis of recombinant HA ectodomain to compare the differences among recombinant trimeric HA proteins from early 2009 pandemic H1N1 viruses, which dissociate to monomers, with those of more recent virus HAs that can be expressed as trimers. We analyzed differences among the HA sequences and identified intermolecular interactions mediated by the residue at position 374 (HA0 numbering) of the HA2 subdomain as critical for HA trimer stability. Crystallographic analyses of HA from the recent H1N1 virus A/Washington/5/2011 highlight the structural basis for this observed phenotype. It remains to be seen whether more recent viruses with this mutation will yield more stable vaccines in the future.

PubMed: 24522930
DOI: 10.1128/JVI.02278-13

実験手法

X-RAY DIFFRACTION (3 Å)