Crystal structure of a fully glycosylated HIV‐1 gp120 core reveals a stabilizing role for the glycan at Asn262. Issue 3 (22nd January 2015)

• Record Type: Journal Article
• Authors: Kong, Leopold; Wilson, Ian A.; Kwong, Peter D.
• Is Part Of: Proteins. Volume 83:Issue 3(2015)
• Page Start: 590
• Page End: 596
• Publication Date: 2015-01-22
• Subjects: Proteins -- Periodicals; Proteins -- Periodicals; 572.6
• DOI: 10.1002/prot.24747
• Languages: English
• ISSNs: 0887-3585

Abstract

<abstract abstract-type="main"> <title>ABSTRACT</title> <p>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 <italic>N</italic>‐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 GlcNAc₂Man₇ 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. Proteins 2015; 83:590–596. © 2014 Wiley Periodicals, Inc.</p> </abstract>