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TitleCovalently linked dengue virus envelope glycoprotein dimers reduce exposure of the immunodominant fusion loop epitope.
Journal, issue, pagesNat Commun, Vol. 8, Page 15411-15411, Year 2017
Publish dateFeb 2, 2017 (structure data deposition date)
AuthorsRouvinski, A. / Dejnirattisai, W. / Guardado-Calvo, P. / Vaney, M.C. / Sharma, A. / Duquerroy, S. / Supasa, P. / Wongwiwat, W. / Haouz, A. / Barba-Spaeth, G. ...Rouvinski, A. / Dejnirattisai, W. / Guardado-Calvo, P. / Vaney, M.C. / Sharma, A. / Duquerroy, S. / Supasa, P. / Wongwiwat, W. / Haouz, A. / Barba-Spaeth, G. / Mongkolsapaya, J. / Rey, F.A. / Screaton, G.R.
External linksNat Commun / PubMed:28534525
MethodsX-ray diffraction
Resolution3.9 Å
Structure data

PDB-5n09:
Crystal structure of L107C/A313C covalently linked dengue 2 virus envelope glycoprotein dimer in complex with the Fab fragment of the broadly neutralizing human antibody EDE2 A11
Method: X-RAY DIFFRACTION / Resolution: 3.9 Å

PDB-5n0a:
Crystal structure of A259C covalently linked dengue 2 virus envelope glycoprotein dimer in complex with the Fab fragment of the broadly neutralizing human antibody EDE2 A11
Method: X-RAY DIFFRACTION / Resolution: 3.9 Å

Chemicals

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

ChemComp-HOH:
WATER

Source
  • dengue virus 2
  • homo sapiens (human)
KeywordsImmune System/Viral Protein / IMMUNE SYSTEM-VIRAL PROTEIN COMPLEX / VIRAL PROTEIN / MEMBRANE FUSION / CLASS 2 FUSION PROTEIN / DENGUE VIRUS / BROADLY NEUTRALIZING ANTIBODY / FAB FRAGMENT / ENVELOPE FUSION PROTEIN

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