Crystallographic studies of ligand binding by Zn-alpha2-glycoprotein.

@article{Delker2004CrystallographicSO,
  title={Crystallographic studies of ligand binding by Zn-alpha2-glycoprotein.},
  author={Silvia L. Delker and Anthony P. West and Lindsay Claire McDermott and Malcolm W Kennedy and Pamela J. Bjorkman},
  journal={Journal of structural biology},
  year={2004},
  volume={148 2},
  pages={
          205-13
        }
}
Zn-alpha2-glycoprotein (ZAG) is a 41 kDa soluble protein that is present in most bodily fluids. The previously reported 2.8 A crystal structure of ZAG isolated from human serum demonstrated the structural similarity between ZAG and class I major histocompatibility complex (MHC) molecules and revealed a non-peptidic ligand in the ZAG counterpart of the MHC peptide-binding groove. Here we present crystallographic studies to explore further the nature of the non-peptidic ligand in the ZAG groove… CONTINUE READING

Citations

Publications citing this paper.
SHOWING 1-10 OF 16 CITATIONS

Similar Papers

Loading similar papers…