3EYM
Structure of Influenza Haemagglutinin in complex with an inhibitor of membrane fusion
Summary for 3EYM
| Entry DOI | 10.2210/pdb3eym/pdb |
| Related | 3EYJ 3EYM |
| Descriptor | Hemagglutinin HA1 chain, Hemagglutinin HA2 chain, 2-tert-butylbenzene-1,4-diol (3 entities in total) |
| Functional Keywords | influenza, hemagglutinin, inhibitor, envelope protein, fusion protein, glycoprotein, lipoprotein, membrane, palmitate, transmembrane, virion, viral protein |
| Biological source | Influenza A virus More |
| Cellular location | Virion membrane; Single-pass type I membrane protein (Potential): P03437 P03437 |
| Total number of polymer chains | 6 |
| Total formula weight | 166344.00 |
| Authors | Russell, R.J.,Kerry, P.S.,Stevens, D.A.,Steinhauer, D.A.,Martin, S.R.,Gamblin, S.J.,Skehel, J.J. (deposition date: 2008-10-21, release date: 2009-01-13, Last modification date: 2024-11-20) |
| Primary citation | Russell, R.J.,Kerry, P.S.,Stevens, D.J.,Steinhauer, D.A.,Martin, S.R.,Gamblin, S.J.,Skehel, J.J. Structure of influenza hemagglutinin in complex with an inhibitor of membrane fusion Proc.Natl.Acad.Sci.USA, 105:17736-17741, 2008 Cited by PubMed Abstract: The influenza surface glycoprotein hemagglutinin (HA) is a potential target for antiviral drugs because of its key roles in the initial stages of infection: receptor binding and the fusion of virus and cell membranes. The structure of HA in complex with a known inhibitor of membrane fusion and virus infectivity, tert-butyl hydroquinone (TBHQ), shows that the inhibitor binds in a hydrophobic pocket formed at an interface between HA monomers. Occupation of this site by TBHQ stabilizes the neutral pH structure through intersubunit and intrasubunit interactions that presumably inhibit the conformational rearrangements required for membrane fusion. The nature of the binding site suggests routes for the chemical modification of TBHQ that could lead to the development of more potent inhibitors of membrane fusion and potential anti-influenza drugs. PubMed: 19004788DOI: 10.1073/pnas.0807142105 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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