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TitleNatively glycosylated HIV-1 Env structure reveals new mode for antibody recognition of the CD4-binding site.
Journal, issue, pagesNat. Struct. Mol. Biol., Vol. 23, Page 906-915, Year 2016
Publish dateAug 26, 2016 (structure data deposition date)
AuthorsGristick, H.B. / von Boehmer, L. / West, A.P. / Schamber, M. / Gazumyan, A. / Golijanin, J. / Seaman, M.S. / Fatkenheuer, G. / Klein, F. / Nussenzweig, M.C. / Bjorkman, P.J.
External linksNat. Struct. Mol. Biol. / PubMed:27617431
MethodsX-ray diffraction
Resolution3.5 - 3.9 Å
Structure data

PDB-5t3x:
3.9 Angstrom Crystal Structure of a Fully and Natively Glycosylated BG505 SOSIP.664 HIV-1 Env Trimer in Complex with the Broadly Neutralizing Antibodies IOMA and 10-1074.
Method: X-RAY DIFFRACTION / Resolution: 3.9 Å

PDB-5t3z:
3.5 Angstrom Crystal Structure of a Fully and Natively Glycosylated BG505 SOSIP.664 HIV-1 Env Trimer in Complex with the Broadly Neutralizing Antibodies IOMA and 10-1074
Method: X-RAY DIFFRACTION / Resolution: 3.5 Å

Chemicals

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

Source
  • human immunodeficiency virus 1
  • homo sapiens (human)
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / HIV / N-linked Glycosylation / Broadly Neutralizing Antibodies / VIRAL PROTEIN-IMMUNE SYSTEM complex

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