2FK0
Crystal Structure of a H5N1 influenza virus hemagglutinin.
Summary for 2FK0
| Entry DOI | 10.2210/pdb2fk0/pdb |
| Descriptor | hemagglutinin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | glycoprotein, membrane-fusion precursor, viral protein |
| Biological source | Influenza A virus (A/Viet Nam/1203/2004(H5N1)) More |
| Total number of polymer chains | 18 |
| Total formula weight | 536738.95 |
| Authors | Stevens, J.,Wilson, I.A. (deposition date: 2006-01-03, release date: 2006-05-02, Last modification date: 2024-11-20) |
| Primary citation | Stevens, J.,Blixt, O.,Tumpey, T.M.,Taubenberger, J.K.,Paulson, J.C.,Wilson, I.A. Structure and Receptor Specificity of the Hemagglutinin from an H5N1 Influenza Virus. Science, 312:404-410, 2006 Cited by PubMed Abstract: The hemagglutinin (HA) structure at 2.9 angstrom resolution, from a highly pathogenic Vietnamese H5N1 influenza virus, is more related to the 1918 and other human H1 HAs than to a 1997 duck H5 HA. Glycan microarray analysis of this Viet04 HA reveals an avian alpha2-3 sialic acid receptor binding preference. Introduction of mutations that can convert H1 serotype HAs to human alpha2-6 receptor specificity only enhanced or reduced affinity for avian-type receptors. However, mutations that can convert avian H2 and H3 HAs to human receptor specificity, when inserted onto the Viet04 H5 HA framework, permitted binding to a natural human alpha2-6 glycan, which suggests a path for this H5N1 virus to gain a foothold in the human population. PubMed: 16543414DOI: 10.1126/science.1124513 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.95 Å) |
Structure validation
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