Human immunoglobulin E flexes between acutely bent and extended conformations

@inproceedings{Drinkwater2014HumanIE,
  title={Human immunoglobulin E flexes between acutely bent and extended conformations},
  author={Nyssa Drinkwater and Ben Cossins and Anthony H Keeble and Michael J Wright and Katharine L Cain and Hanna Hailu and Amanda K F Oxbrow and Jean Delgado and Lindsay K Shuttleworth and Michael W-P Kao and James M McDonnell and Andrew J Beavil and Alistair J Henry and Brian J. Sutton},
  booktitle={Nature Structural &Molecular Biology},
  year={2014}
}
Crystallographic and solution studies have shown that IgE molecules are acutely bent in their Fc region. Crystal structures reveal the Cɛ2 domain pair folded back onto the Cɛ3-Cɛ4 domains, but is the molecule exclusively bent or can the Cɛ2 domains adopt extended conformations and even 'flip' from one side of the molecule to the other? We report the crystal structure of IgE-Fc captured in a fully extended, symmetrical conformation and show by molecular dynamics, calorimetry, stopped-flow… CONTINUE READING
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