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4RQS

Crystal structure of fully glycosylated HIV-1 gp120 core bound to CD4 and 17b Fab

Summary for 4RQS
Entry DOI10.2210/pdb4rqs/pdb
Descriptor2-domain CD4, 17b Fab Light Chain, 17b Fab Heavy Chain, ... (8 entities in total)
Functional Keywordsimmunoglobulin fold, n-linked glycosylation, immune system
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains4
Total formula weight108437.06
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 citationKong, 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: 25546301
DOI: 10.1002/prot.24747
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (4.493 Å)
Structure validation

226707

數據於2024-10-30公開中

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