Crystal structure of a fully glycosylated HIV-1 gp120 core reveals a stabilizing role for the glycan at Asn262
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. Lastly, 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.
- Authors:
-
- National Inst. of Health (NIH), Bethesda, MD (United States). Vaccine Research Center; Scripps Research Inst., La Jolla, CA (United States). Dept. of Integrative Structural and Computational Biology; Scripps Research Inst., La Jolla, CA (United States). International AIDS Vaccine Initiative Neutralizing Antibody Center; Scripps Research Inst., La Jolla, CA (United States). Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery
- Scripps Research Inst., La Jolla, CA (United States). Dept. of Integrative Structural and Computational Biology; Scripps Research Inst., La Jolla, CA (United States). International AIDS Vaccine Initiative Neutralizing Antibody Center; Scripps Research Inst., La Jolla, CA (United States). Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery; Scripps Research Inst., La Jolla, CA (United States). Skaggs Inst. for Chemical Biology
- National Inst. of Health (NIH), Bethesda, MD (United States). Vaccine Research Center
- Publication Date:
- Research Org.:
- Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES)
- OSTI Identifier:
- 1170033
- Grant/Contract Number:
- W-31-109-Eng-38; RO1 AI084817; GM U54 GM94586; UM1 AI100663
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Proteins
- Additional Journal Information:
- Journal Volume: 83; Journal Issue: 3; Journal ID: ISSN 0887-3585
- Publisher:
- Wiley
- Country of Publication:
- United States
- Language:
- ENGLISH
- Subject:
- 60 APPLIED LIFE SCIENCES; HIV-1 gp120; glycan shield; role of N262
Citation Formats
Kong, Leopold, Wilson, Ian A., and Kwong, Peter D. Crystal structure of a fully glycosylated HIV-1 gp120 core reveals a stabilizing role for the glycan at Asn262. United States: N. p., 2014.
Web. doi:10.1002/prot.24747.
Kong, Leopold, Wilson, Ian A., & Kwong, Peter D. Crystal structure of a fully glycosylated HIV-1 gp120 core reveals a stabilizing role for the glycan at Asn262. United States. https://doi.org/10.1002/prot.24747
Kong, Leopold, Wilson, Ian A., and Kwong, Peter D. Fri .
"Crystal structure of a fully glycosylated HIV-1 gp120 core reveals a stabilizing role for the glycan at Asn262". United States. https://doi.org/10.1002/prot.24747. https://www.osti.gov/servlets/purl/1170033.
@article{osti_1170033,
title = {Crystal structure of a fully glycosylated HIV-1 gp120 core reveals a stabilizing role for the glycan at Asn262},
author = {Kong, Leopold and Wilson, Ian A. and Kwong, Peter D.},
abstractNote = {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. Lastly, 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.},
doi = {10.1002/prot.24747},
journal = {Proteins},
number = 3,
volume = 83,
place = {United States},
year = {Fri Dec 26 00:00:00 EST 2014},
month = {Fri Dec 26 00:00:00 EST 2014}
}
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