2VSK
Hendra virus attachment glycoprotein in complex with human cell surface receptor ephrinB2
Summary for 2VSK
| Entry DOI | 10.2210/pdb2vsk/pdb |
| Related | 2VSM |
| Descriptor | HEMAGGLUTININ-NEURAMINIDASE, EPHRIN-B2 (2 entities in total) |
| Functional Keywords | developmental protein, henipavirus, neurogenesis, glycoprotein, paramyxovirus, envelope protein, cell surface receptor, hendra, virion, ephrin, complex, membrane, hydrolase, b2, efn, niv, eph, hev, hev-g, nipah, virus, niv-g, phosphoprotein, differentiation, viral attachment, signal-anchor, hemagglutinin, transmembrane |
| Biological source | Hendra virus More |
| Cellular location | Virion membrane ; Single-pass type II membrane protein : O89343 Membrane; Single-pass type I membrane protein: P52799 |
| Total number of polymer chains | 4 |
| Total formula weight | 125106.38 |
| Authors | Bowden, T.A.,Aricescu, A.R.,Gilbert, R.J.,Grimes, J.M.,Jones, E.Y.,Stuart, D.I. (deposition date: 2008-04-24, release date: 2008-05-20, Last modification date: 2024-11-13) |
| Primary citation | Bowden, T.A.,Aricescu, A.R.,Gilbert, R.J.,Grimes, J.M.,Jones, E.Y.,Stuart, D.I. Structural Basis of Nipah and Hendra Virus Attachment to Their Cell-Surface Receptor Ephrin-B2 Nat.Struct.Mol.Biol., 15:567-, 2008 Cited by PubMed Abstract: Nipah and Hendra viruses are emergent paramyxoviruses, causing disease characterized by rapid onset and high mortality rates, resulting in their classification as Biosafety Level 4 pathogens. Their attachment glycoproteins are essential for the recognition of the cell-surface receptors ephrin-B2 (EFNB2) and ephrin-B3 (EFNB3). Here we report crystal structures of both Nipah and Hendra attachment glycoproteins in complex with human EFNB2. In contrast to previously solved paramyxovirus attachment complexes, which are mediated by sialic acid interactions, the Nipah and Hendra complexes are maintained by an extensive protein-protein interface, including a crucial phenylalanine side chain on EFNB2 that fits snugly into a hydrophobic pocket on the viral protein. By analogy with the development of antivirals against sialic acid binding viruses, these results provide a structural template to target antiviral inhibition of protein-protein interactions. PubMed: 18488039DOI: 10.1038/NSMB.1435 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.3 Å) |
Structure validation
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