1RVT
1930 H1 Hemagglutinin in complex with LSTC
Summary for 1RVT
Entry DOI | 10.2210/pdb1rvt/pdb |
Related | 1RU7 1RUY 1RUZ 1RV0 1RVX 1RVZ |
Descriptor | hemagglutinin, N-acetyl-alpha-neuraminic acid-(2-6)-beta-D-galactopyranose, N-acetyl-alpha-neuraminic acid-(2-6)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, ... (6 entities in total) |
Functional Keywords | hemagglutinin, influenza a virus, viral protein |
Biological source | unidentified influenza virus More |
Total number of polymer chains | 6 |
Total formula weight | 165329.64 |
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: 2003-12-15, release date: 2004-03-30, Last modification date: 2024-10-09) |
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 Cited by 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: 14764886DOI: 10.1126/science.1093155 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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