Published March 19, 1999
| public
Journal Article
Crystal Structure of Human ZAG, a Fat-Depleting Factor Related to MHC Molecules
Chicago
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Abstract
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.
Additional Information
© 1999 American Association for the Advancement of Science. Received 21 December 1998; accepted 18 February 1999. We thank G. Hathaway, P. G. Green, and K. Faull for mass spectrometric analyses. ZAG coordinates have been deposited in the PDB (code 1zag). L.M.S. was supported by a grant from the U.S. Department of Defense Breast Cancer Research Program.Additional details
- Eprint ID
- 52060
- DOI
- 10.1126/science.283.5409.1914
- Resolver ID
- CaltechAUTHORS:20141121-150058081
- Department of Defense Breast Cancer Research Program
- Created
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2014-11-21Created from EPrint's datestamp field
- Updated
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2021-11-10Created from EPrint's last_modified field