Crystal structure of a fully glycosylated HIV-1 gp120 core reveals a stabilizing role for the glycan at Asn262 [electronic resource]

• Ngôn ngữ: eng
• Thông tin xuất bản: Washington, D.C. : Oak Ridge, Tenn. : United States. Dept. of Energy. Office of Science ; Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy, 2014
• Mô tả vật lý: Size: p. 590-596 : , digital, PDF file.
• Bộ sưu tập: Metadata
• ID: 261306
• Chủ đề: 1. 60 applied life sciences; 2. Glycan shield; 3. Hiv-1 gp120; 4. Role of n262

Tóm tắt

 The crystal structure of a fully glycosylated HIV-1 gp120 core in complex with CD4 receptor and Fab 17b at 4.5-� 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<
 sub>
 2<
 /sub>
 Man<
 sub>
 7<
 /sub>
  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.