7A9D
Crystal structure of H12 Haemagglutinin
Summary for 7A9D
Entry DOI | 10.2210/pdb7a9d/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 | receptor binding, fusion of virus membrane with host plasma membrane., viral protein |
Biological source | Influenza A virus (A/duck/Alberta/60/1976(H12N5)) More |
Total number of polymer chains | 4 |
Total formula weight | 113148.40 |
Authors | Xiong, X.,Walker, P.,Zhang, J.,Gamblin, S.,Skehel, J.J. (deposition date: 2020-09-01, release date: 2020-12-02, Last modification date: 2024-11-13) |
Primary citation | Gamblin, S.J.,Vachieri, S.G.,Xiong, X.,Zhang, J.,Martin, S.R.,Skehel, J.J. Hemagglutinin Structure and Activities. Cold Spring Harb Perspect Med, 11:-, 2021 Cited by PubMed Abstract: Hemagglutinins (HAs) are the receptor-binding and membrane fusion glycoproteins of influenza viruses. They recognize sialic acid-containing, cell-surface glycoconjugates as receptors but have limited affinity for them, and, as a consequence, virus attachment to cells requires their interaction with several virus HAs. Receptor-bound virus is transferred into endosomes where membrane fusion by HAs is activated at pH between 5 and 6.5, depending on the strain of virus. Fusion activity requires extensive rearrangements in HA conformation that include extrusion of a buried "fusion peptide" to connect with the endosomal membrane, form a bridge to the virus membrane, and eventually bring both membranes close together. In this review, we give an overview of the structures of the 16 genetically and antigenically distinct subtypes of influenza A HA in relation to these two functions in virus replication and in relation to recognition of HA by antibodies that neutralize infection. PubMed: 32513673DOI: 10.1101/cshperspect.a038638 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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