Natively glycosylated HIV-1 Env structure reveals new mode for antibody recognition of the CD4-binding site-Reference-Cited by-同舟云学术

Natively glycosylated HIV-1 Env structure reveals new mode for antibody recognition of the CD4-binding site

Published:2016-09-12 Issue:10 Volume:23 Page:906-915
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Gristick Harry B,von Boehmer Lotta,West Jr Anthony P,Schamber Michael,Gazumyan Anna,Golijanin Jovana,Seaman Michael S,Fätkenheuer Gerd,Klein Florian,Nussenzweig Michel C,Bjorkman Pamela J

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

http://www.nature.com/articles/nsmb.3291.pdf

Reference62 articles.

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2. Kwong, P.D. et al. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 393, 648–659 (1998).

3. Julien, J.P. et al. Crystal structure of a soluble cleaved HIV-1 envelope trimer. Science 342, 1477–1483 (2013).

4. Pancera, M. et al. Structure and immune recognition of trimeric pre-fusion HIV-1 Env. Nature 514, 455–461 (2014).

5. Scharf, L. et al. Broadly neutralizing antibody 8ANC195 recognizes closed and open states of HIV-1 Env. Cell 162, 1379–1390 (2015).

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