4RQS
Crystal structure of fully glycosylated HIV-1 gp120 core bound to CD4 and 17b Fab
Summary for 4RQS
Entry DOI | 10.2210/pdb4rqs/pdb |
Descriptor | 2-domain CD4, 17b Fab Light Chain, 17b Fab Heavy Chain, ... (8 entities in total) |
Functional Keywords | immunoglobulin fold, n-linked glycosylation, immune system |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 4 |
Total formula weight | 108437.06 |
Authors | Kong, L.,Wilson, I.A.,Kwong, P.D. (deposition date: 2014-11-05, release date: 2014-12-31, Last modification date: 2024-10-09) |
Primary citation | Kong, L.,Wilson, I.A.,Kwong, P.D. Crystal structure of a fully glycosylated HIV-1 gp120 core reveals a stabilizing role for the glycan at Asn262. Proteins, 83:590-596, 2015 Cited by PubMed Abstract: 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. PubMed: 25546301DOI: 10.1002/prot.24747 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (4.493 Å) |
Structure validation
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