4LXV
Crystal Structure of the Hemagglutinin from a H1N1pdm A/WASHINGTON/5/2011 virus
Summary for 4LXV
Entry DOI | 10.2210/pdb4lxv/pdb |
Descriptor | 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) |
Functional Keywords | hemagglutinin, pandemic, influenza, viral protein |
Biological source | Influenza A virus More |
Total number of polymer chains | 12 |
Total formula weight | 350147.70 |
Authors | 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. (deposition date: 2013-07-30, release date: 2014-02-26, Last modification date: 2024-10-16) |
Primary citation | 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 Cited by 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: 24522930DOI: 10.1128/JVI.02278-13 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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