Crystal Structure of Human ZAG, a Fat-Depleting Factor Related to MHC Molecules
Copyright policy )Crystal Structure of Human ZAG, a Fat-Depleting Factor Related to MHC Molecules
Zn-α 2 -glycoprotein (ZAG) is a soluble protein that is present in serum and other body fluids. ZAG stimulates lipid degradation in adipocytes and causes the extensive fat losses associated with some advanced cancers. The 2.8 angstrom crystal structure of ZAG resembles a class I major histocompatibility complex (MHC) heavy chain, but ZAG does not bind the class I light chain β 2 -microglobulin. The ZAG structure includes a large groove analogous to class I MHC peptide binding grooves. Instead of a peptide, the ZAG groove contains a nonpeptidic compound that may be implicated in lipid catabolism under normal or pathological conditions.
- Howard Hughes Medical Institute United States
- California Institute of Technology United States
Models, Molecular, 570, Protein Folding, Binding Sites, Glycosylation, Protein Conformation, Histocompatibility Antigens Class I, Seminal Plasma Proteins, Hydrogen Bonding, Crystallography, X-Ray, Ligands, Lipid Metabolism, Zn-Alpha-2-Glycoprotein, Protein Structure, Secondary, Protein Structure, Tertiary, HLA-A2 Antigen, Humans, Peptides, beta 2-Microglobulin, Glycoproteins, Protein Binding
Models, Molecular, 570, Protein Folding, Binding Sites, Glycosylation, Protein Conformation, Histocompatibility Antigens Class I, Seminal Plasma Proteins, Hydrogen Bonding, Crystallography, X-Ray, Ligands, Lipid Metabolism, Zn-Alpha-2-Glycoprotein, Protein Structure, Secondary, Protein Structure, Tertiary, HLA-A2 Antigen, Humans, Peptides, beta 2-Microglobulin, Glycoproteins, Protein Binding
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