1RV0

1930 Swine H1 Hemagglutinin complexed with LSTA

Summary for 1RV0

• Entry DOI: 10.2210/pdb1rv0/pdb
• Related: 1RU7 1RUY 1RUZ 1RVT 1RVX 1RVZ
• Descriptor: hemagglutinin, 2-acetamido-2-deoxy-alpha-D-glucopyranose, 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID, ... (5 entities in total)
• Functional Keywords: hemagglutinin, influenza a virus, viral protein
• Biological source: Influenza A virus; More
• Total number of polymer chains: 6
• Total formula weight: 163724.09

Authors

Skehel, J.J.,Gamblin, S.J.,Haire, L.F.,Russell, R.J.,Stevens, D.J.,Xiao, B.,Ha, Y.,Vasisht, N.,Steinhauer, D.A.,Daniels, R.S. (deposition date: 2003-12-12, release date: 2004-03-30, Last modification date: 2024-10-30)

Primary citation

Gamblin, S.J.,Haire, L.F.,Russell, R.J.,Stevens, D.J.,Xiao, B.,Ha, Y.,Vasisht, N.,Steinhauer, D.A.,Daniels, R.S.,Elliot, A.,Wiley, D.C.,Skehel, J.J.
The structure and receptor binding properties of the 1918 influenza hemagglutinin.
Science, 303:1838-1842, 2004

PubMed Abstract: The 1918 influenza pandemic resulted in about 20 million deaths. This enormous impact, coupled with renewed interest in emerging infections, makes characterization of the virus involved a priority. Receptor binding, the initial event in virus infection, is a major determinant of virus transmissibility that, for influenza viruses, is mediated by the hemagglutinin (HA) membrane glycoprotein. We have determined the crystal structures of the HA from the 1918 virus and two closely related HAs in complex with receptor analogs. They explain how the 1918 HA, while retaining receptor binding site amino acids characteristic of an avian precursor HA, is able to bind human receptors and how, as a consequence, the virus was able to spread in the human population.

PubMed: 14764886
DOI: 10.1126/science.1093155

Experimental method

X-RAY DIFFRACTION (2.5 Å)