Crystal structure of a fully glycosylated HIV‐1 gp120 core reveals a stabilizing role for the glycan at Asn262 |
| |
| Authors: | Leopold Kong Ian A Wilson Peter D Kwong |
| |
| Institution: | 1. Vaccine Research Center, National Institutes of Health, Bethesda, Maryland;2. Department of Integrative Structural and Computational Biology, the Scripps Research Institute, La Jolla, California;3. International AIDS Vaccine Initiative Neutralizing Antibody Center and the Collaboration for AIDS Vaccine Discovery, the Scripps Research Institute, La Jolla, California;4. Scripps Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery, the Scripps Research Institute, La Jolla, California;5. Skaggs Institute for Chemical Biology, the Scripps Research Institute, La Jolla, California |
| |
| 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 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. |
| |
| Keywords: | HIV‐1 gp120 glycan shield role of N262 |
|
|
