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Structure paper

TitleStructural Basis of Nipah and Hendra Virus Attachment to Their Cell-Surface Receptor Ephrin-B2
Journal, issue, pagesNat. Struct. Mol. Biol., Vol. 15, Page 567-, Year 2008
Publish dateApr 24, 2008 (structure data deposition date)
AuthorsBowden, T.A. / Aricescu, A.R. / Gilbert, R.J. / Grimes, J.M. / Jones, E.Y. / Stuart, D.I.
External linksNat. Struct. Mol. Biol. / PubMed:18488039
MethodsX-ray diffraction
Resolution1.8 - 3.3 Å
Structure data

PDB-2vsk:
Hendra virus attachment glycoprotein in complex with human cell surface receptor ephrinB2
Method: X-RAY DIFFRACTION / Resolution: 3.3 Å

PDB-2vsm:
Nipah virus attachment glycoprotein in complex with human cell surface receptor ephrinB2
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-IPA:
ISOPROPYL ALCOHOL / alkaloid*YM

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-HOH:
WATER

Source
  • hendra virus
  • homo sapiens (human)
  • nipah virus
KeywordsHYDROLASE / DEVELOPMENTAL PROTEIN / HENIPAVIRUS / NEUROGENESIS / GLYCOPROTEIN / PARAMYXOVIRUS / ENVELOPE PROTEIN / CELL SURFACE RECEPTOR / HENDRA / VIRION / EPHRIN / COMPLEX / MEMBRANE / B2 / EFN / NIV / EPH / HEV / HEV-G / NIPAH / VIRUS / NIV-G / PHOSPHOPROTEIN / DIFFERENTIATION / VIRAL ATTACHMENT / SIGNAL-ANCHOR / HEMAGGLUTININ / TRANSMEMBRANE

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