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1RVZ

1934 H1 Hemagglutinin in complex with LSTC

Summary for 1RVZ
Entry DOI10.2210/pdb1rvz/pdb
Related1RU7 1RUY 1RUZ 1RV0 1RVT 1RVX
Related PRD IDPRD_900046
Descriptorhemagglutinin, N-acetyl-alpha-neuraminic acid-(2-6)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
Functional Keywordshemagglutinin, influenza a virus, viral protein
Biological sourceInfluenza A virus (A/Puerto Rico/8/34(H1N1))
More
Cellular locationHost apical cell membrane ; Single-pass type I membrane protein . Virion membrane ; Single-pass type I membrane protein : Q82766 Q82766
Total number of polymer chains12
Total formula weight334564.99
Authors
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. (deposition date: 2003-12-15, release date: 2004-03-30, Last modification date: 2024-10-30)
Primary citationGamblin, 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: 14764886
DOI: 10.1126/science.1093155
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.25 Å)
Structure validation

226707

건을2024-10-30부터공개중

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