PMID- 10206894 OWN - NLM STAT- MEDLINE DCOM- 19990413 LR - 20190619 IS - 0036-8075 (Print) IS - 0036-8075 (Linking) VI - 283 IP - 5409 DP - 1999 Mar 19 TI - Crystal structure of human ZAG, a fat-depleting factor related to MHC molecules. PG - 1914-9 AB - 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. FAU - Sanchez, L M AU - Sanchez LM AD - Division of Biology, California Institute of Technology, Pasadena, CA 91125, USA. FAU - Chirino, A J AU - Chirino AJ FAU - Bjorkman, P j AU - Bjorkman Pj LA - eng SI - PDB/1ZAG PT - Journal Article PL - United States TA - Science JT - Science (New York, N.Y.) JID - 0404511 RN - 0 (Glycoproteins) RN - 0 (HLA-A2 Antigen) RN - 0 (Histocompatibility Antigens Class I) RN - 0 (Ligands) RN - 0 (Peptides) RN - 0 (Seminal Plasma Proteins) RN - 0 (Zn-alpha-2-glycoprotein) RN - 0 (beta 2-Microglobulin) SB - IM MH - Binding Sites MH - Crystallography, X-Ray MH - Glycoproteins/blood/*chemistry/isolation & purification/metabolism MH - Glycosylation MH - HLA-A2 Antigen/chemistry/metabolism MH - Histocompatibility Antigens Class I/*chemistry MH - Humans MH - Hydrogen Bonding MH - Ligands MH - Lipid Metabolism MH - Models, Molecular MH - Peptides/metabolism MH - Protein Binding MH - Protein Conformation MH - Protein Folding MH - Protein Structure, Secondary MH - Protein Structure, Tertiary MH - *Seminal Plasma Proteins MH - beta 2-Microglobulin/metabolism EDAT- 1999/04/17 00:00 MHDA- 1999/04/17 00:01 CRDT- 1999/04/17 00:00 PHST- 1999/04/17 00:00 [pubmed] PHST- 1999/04/17 00:01 [medline] PHST- 1999/04/17 00:00 [entrez] AID - 10.1126/science.283.5409.1914 [doi] PST - ppublish SO - Science. 1999 Mar 19;283(5409):1914-9. doi: 10.1126/science.283.5409.1914.