Aromatic residues at the edge of the antibody combining site facilitate viral glycoprotein recognition through membrane interactions.

@article{Scherer2010AromaticRA,
  title={Aromatic residues at the edge of the antibody combining site facilitate viral glycoprotein recognition through membrane interactions.},
  author={Erin M. Scherer and Daniel P. Leaman and Michael B. Zwick and Andrew J McMichael and Dennis R. Burton},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2010},
  volume={107 4},
  pages={1529-34}
}
The broadly neutralizing anti-HIV antibody 4E10 recognizes an epitope very close to the virus membrane on the glycoprotein gp41. It was previously shown that epitope recognition improves in a membrane context and that 4E10 binds directly, albeit weakly, to lipids. Furthermore, a crystal structure of Fab 4E10 complexed to an epitope peptide revealed that the centrally placed, protruding H3 loop of the antibody heavy chain does not form peptide contacts. To investigate the hypothesis that the H3… CONTINUE READING

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