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HIV-1 gp120 核心全糖基化的晶体结构揭示了糖基在 Asn262 处的稳定作用。

Crystal structure of a fully glycosylated HIV-1 gp120 core reveals a stabilizing role for the glycan at Asn262.

机构信息

Vaccine Research Center, National Institutes of Health, Bethesda, Maryland, 20892; Department of Integrative Structural and Computational Biology, the Scripps Research Institute, La Jolla, California; International AIDS Vaccine Initiative Neutralizing Antibody Center and the Collaboration for AIDS Vaccine Discovery, the Scripps Research Institute, La Jolla, California; Scripps Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery, the Scripps Research Institute, La Jolla, California.

出版信息

Proteins. 2015 Mar;83(3):590-6. doi: 10.1002/prot.24747. Epub 2015 Jan 22.

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.

摘要

HIV-1 gp120 核心的全糖基化复合物与 CD4 受体和 Fab 17b 的晶体结构,分辨率为 4.5埃,揭示了核心 gp120 的 15 个 N 连接聚糖中的 9 个是部分有序的。位置 Asn262 的聚糖具有最广泛和最有序的电子密度,并对 GlcNAc(2)Man(7)进行了建模。该聚糖的 GlcNAc 主干大部分埋藏在 gp120 的裂缝中,表明其在 gp120 折叠和稳定性中发挥作用。它的臂与寡甘露糖补丁中相邻聚糖的主干相互作用,寡甘露糖补丁是广泛中和抗体的主要靶标。

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