Crystal structure of a fully glycosylated HIV-1 gp120 core reveals a stabilizing role for the glycan at Asn262

Proteins. 2015 Mar;83(3):590-6. doi: 10.1002/prot.24747. Epub 2015 Jan 22.


The crystal structure of a fully glycosylated HIV-1 gp120 core in complex with CD4 receptor and Fab 17b at 4.5-Å resolution reveals 9 of the 15 N-linked glycans of core gp120 to be partially ordered. The glycan at position Asn262 had the most extensive and well-ordered electron density, and a GlcNAc(2)Man(7) was modeled. The GlcNAc stem of this glycan is largely buried in a cleft in gp120, suggesting a role in gp120 folding and stability. Its arms interact with the stems of neighboring glycans from the oligomannose patch, which is a major target for broadly neutralizing antibodies.

Keywords: HIV-1 gp120; glycan shield; role of N262.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, N.I.H., Intramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Asparagine / chemistry*
  • Asparagine / metabolism*
  • Binding Sites, Antibody
  • CD4 Antigens / chemistry
  • CD4 Antigens / metabolism
  • Crystallography, X-Ray
  • Glycosylation
  • HEK293 Cells
  • HIV Envelope Protein gp120 / chemistry*
  • HIV Envelope Protein gp120 / metabolism
  • HIV-1 / chemistry
  • Humans
  • Mannose / chemistry
  • Models, Molecular
  • Polysaccharides / chemistry*
  • Polysaccharides / metabolism


  • CD4 Antigens
  • HIV Envelope Protein gp120
  • Polysaccharides
  • Asparagine
  • Mannose