1ZAG
HUMAN ZINC-ALPHA-2-GLYCOPROTEIN
Summary for 1ZAG
Entry DOI | 10.2210/pdb1zag/pdb |
Descriptor | PROTEIN (ZINC-ALPHA-2-GLYCOPROTEIN), 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, N-acetyl-alpha-neuraminic acid-(2-6)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total) |
Functional Keywords | lipid mobilization factor, secreted mhc class i homolog |
Biological source | Homo sapiens (human) |
Total number of polymer chains | 4 |
Total formula weight | 132606.04 |
Authors | Chirino, A.J.,Sanchez, L.M.,Bjorkman, P.J. (deposition date: 1999-02-02, release date: 1999-03-31, Last modification date: 2023-12-27) |
Primary citation | Sanchez, L.M.,Chirino, A.J.,Bjorkman, P. Crystal structure of human ZAG, a fat-depleting factor related to MHC molecules. Science, 283:1914-1919, 1999 Cited by PubMed Abstract: Zn-alpha2-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 beta2-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. PubMed: 10206894DOI: 10.1126/science.283.5409.1914 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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