Zn-alpha2-glycoprotein, an MHC class I-related glycoprotein regulator of adipose tissues: modification or abrogation of ligand binding by site-directed mutagenesis.

@article{McDermott2006Znalpha2glycoproteinAM,
  title={Zn-alpha2-glycoprotein, an MHC class I-related glycoprotein regulator of adipose tissues: modification or abrogation of ligand binding by site-directed mutagenesis.},
  author={Lindsay C McDermott and June A Freel and Anthony P. West and Pamela J. Bjorkman and Malcolm W Kennedy},
  journal={Biochemistry},
  year={2006},
  volume={45 7},
  pages={2035-41}
}
Zn-alpha(2)-glycoprotein (ZAG) is a soluble lipid-mobilizing factor associated with cancer cachexia and is a novel adipokine. Its X-ray crystal structure reveals a poly(ethylene glycol) molecule, presumably substituting for a higher affinity natural ligand, occupying an apolar groove between its alpha(1) and alpha(2) domain helices that corresponds to the peptide binding groove in class I MHC proteins. We previously provided evidence that the groove is a binding site for hydrophobic ligands… CONTINUE READING