The crystal structure of avian CD1 reveals a smaller, more primordial antigen-binding pocket compared to mammalian CD1.

@article{Zajonc2008TheCS,
  title={The crystal structure of avian CD1 reveals a smaller, more primordial antigen-binding pocket compared to mammalian CD1.},
  author={Dirk M. Zajonc and Harald Striegl and Christopher C. Dascher and Ian A. Wilson},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2008},
  volume={105 46},
  pages={17925-30}
}
The molecular details of glycolipid presentation by CD1 antigen-presenting molecules are well studied in mammalian systems. However, little is known about how these non-classical MHC class I (MHCI) molecules diverged from the MHC locus to create a more complex, hydrophobic binding groove that binds lipids rather than peptides. To address this fundamental question, we have determined the crystal structure of an avian CD1 (chCD1-2) that shares common ancestry with mammalian CD1 from approximately… CONTINUE READING
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