Supersite of immune vulnerability on the glycosylated face of HIV-1 envelope glycoprotein gp120

@article{Kong2013SupersiteOI,
  title={Supersite of immune vulnerability on the glycosylated face of HIV-1 envelope glycoprotein gp120},
  author={Leopold Kong and Jeong Hyun Lee and Katie J. Doores and Charles D. Murin and Jean-Philippe Julien and Ryan McBride and Yan Liu and Andre J. Marozsan and Albert Cupo and Per Johan Klasse and Simon Hoffenberg and Michael P. Caulfield and C. Richter King and Yuanzi Hua and Khoa Le and Reza Khayat and Marc C. Deller and Thomas Clayton and Henry Tien and Ten Feizi and Rogier W. Sanders and James C. Paulson and John P. Moore and Robyn L. Stanfield and Dennis R. Burton and Andrew B. Ward and Ian A. Wilson},
  journal={Nature structural \& molecular biology},
  year={2013},
  volume={20},
  pages={796 - 803}
}
A substantial proportion of the broadly neutralizing antibodies (bnAbs) identified in certain HIV-infected donors recognize glycan-dependent epitopes on HIV-1 gp120. Here we elucidate how the bnAb PGT 135 binds its Asn332 glycan–dependent epitope from its 3.1-Å crystal structure with gp120, CD4 and Fab 17b. PGT 135 interacts with glycans at Asn332, Asn392 and Asn386, using long CDR loops H1 and H3 to penetrate the glycan shield and access the gp120 protein surface. EM reveals that PGT 135 can… 

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TLDR
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TLDR
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TLDR
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TLDR
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