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PMID: 10206894 Published · ppublish English Journal Article

Crystal structure of human ZAG, a fat-depleting factor related to MHC molecules.

Science (New York, N.Y.) ·Vol. 283 ·No. 5409 ·1999-03-19 ·Pages 1914-9

Sánchez LM, Chirino AJ, Bjorkman Pj

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.

MeSH Terms
Binding Sites Crystallography, X-Ray Glycoproteins/blood,chemistry,isolation & purification,metabolism Glycosylation HLA-A2 Antigen/chemistry,metabolism Histocompatibility Antigens Class I/chemistry Humans Hydrogen Bonding Ligands Lipid Metabolism Models, Molecular Peptides/metabolism Protein Binding Protein Conformation Protein Folding Protein Structure, Secondary Protein Structure, Tertiary Seminal Plasma Proteins Zn-Alpha-2-Glycoprotein beta 2-Microglobulin/metabolism
Chemicals
Glycoproteins HLA-A2 Antigen Histocompatibility Antigens Class I Ligands Peptides Seminal Plasma Proteins Zn-Alpha-2-Glycoprotein beta 2-Microglobulin
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Sánchez L M
Division of Biology, California Institute of Technology, Pasadena, CA 91125, USA.
Chirino A J
Bjorkman P j
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1999-03-19
Pages
1914-9
Language
English
Region
United States
NLM ID
0404511
Subset
IM
Databases
PDB
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