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2VSK

Hendra virus attachment glycoprotein in complex with human cell surface receptor ephrinB2

Summary for 2VSK
Entry DOI10.2210/pdb2vsk/pdb
Related2VSM
DescriptorHEMAGGLUTININ-NEURAMINIDASE, EPHRIN-B2 (2 entities in total)
Functional Keywordsdevelopmental 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 sourceHendra virus
More
Cellular locationVirion membrane ; Single-pass type II membrane protein : O89343
Membrane; Single-pass type I membrane protein: P52799
Total number of polymer chains4
Total formula weight125106.38
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 citationBowden, 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: 18488039
DOI: 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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