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TitleStructural and functional analyses reveal promiscuous and species specific use of ephrin receptors by Cedar virus.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 116, Page 20707-20715, Year 2019
Publish dateJun 4, 2019 (structure data deposition date)
AuthorsLaing, E.D. / Navaratnarajah, C.K. / Cheliout Da Silva, S. / Petzing, S.R. / Xu, Y. / Sterling, S.L. / Marsh, G.A. / Wang, L.F. / Amaya, M. / Nikolov, D.B. ...Laing, E.D. / Navaratnarajah, C.K. / Cheliout Da Silva, S. / Petzing, S.R. / Xu, Y. / Sterling, S.L. / Marsh, G.A. / Wang, L.F. / Amaya, M. / Nikolov, D.B. / Cattaneo, R. / Broder, C.C. / Xu, K.
External linksProc. Natl. Acad. Sci. USA / PubMed:31548390
MethodsX-ray diffraction
Resolution2.844 - 3.49 Å
Structure data

PDB-6p72:
Crystal Structure of the Cedar henipavirus Attachment G Glycoprotein global domain
Method: X-RAY DIFFRACTION / Resolution: 3.283 Å

PDB-6p7s:
Crystal Structure of the Cedar henipavirus Attachment G Glycoprotein globular domain in complex with the receptor ephrin-B1
Method: X-RAY DIFFRACTION / Resolution: 3.49 Å

PDB-6p7y:
Crystal Structure of the Cedar henipavirus Attachment G Glycoprotein globular domain in complex with the receptor ephrin-B2
Method: X-RAY DIFFRACTION / Resolution: 2.844 Å

Chemicals

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

ChemComp-HOH:
WATER

Source
  • cedar virus
  • mus musculus (house mouse)
  • homo sapiens (human)
KeywordsVIRAL PROTEIN / Cedar virus / attachment / glycoprotein / G protein / receptor / ephrin-B1 / henipavirus / ephrin-B2

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