Crystal structure of human CD1e reveals a groove suited for lipid-exchange processes.

@article{GarciaAlles2011CrystalSO,
  title={Crystal structure of human CD1e reveals a groove suited for lipid-exchange processes.},
  author={Luis F Garcia-Alles and Gaelle Giacometti and Cees Versluis and Laurent Maveyraud and Diane De Paepe and Julie Guiard and Samuel Tranier and Martine Gilleron and J. Reginaldo Prandi and Daniel Hanau and Albert J. R. Heck and Lucia Mori and Gennaro De Libero and Germain Puzo and Lionel Mourey and Henri de la Salle},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2011},
  volume={108 32},
  pages={
          13230-5
        }
}
CD1e is the only human CD1 protein existing in soluble form in the late endosomes of dendritic cells, where it facilitates the processing of glycolipid antigens that are ultimately recognized by CD1b-restricted T cells. The precise function of CD1e remains undefined, thus impeding efforts to predict the participation of this protein in the presentation of other antigens. To gain insight into its function, we determined the crystal structure of recombinant CD1e expressed in human cells at 2.90… CONTINUE READING

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