1zag

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{{STRUCTURE_1zag| PDB=1zag | SCENE= }}
{{STRUCTURE_1zag| PDB=1zag | SCENE= }}
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'''HUMAN ZINC-ALPHA-2-GLYCOPROTEIN'''
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===HUMAN ZINC-ALPHA-2-GLYCOPROTEIN===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 10206894 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10206894}}
==About this Structure==
==About this Structure==
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[[Category: Lipid mobilization factor]]
[[Category: Lipid mobilization factor]]
[[Category: Secreted mhc class i homolog]]
[[Category: Secreted mhc class i homolog]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:23:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:46:56 2008''

Revision as of 14:47, 28 July 2008

Image:1zag.png

Template:STRUCTURE 1zag

HUMAN ZINC-ALPHA-2-GLYCOPROTEIN

Template:ABSTRACT PUBMED 10206894

About this Structure

1ZAG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of human ZAG, a fat-depleting factor related to MHC molecules., Sanchez LM, Chirino AJ, Bjorkman P, Science. 1999 Mar 19;283(5409):1914-9. PMID:10206894

Page seeded by OCA on Mon Jul 28 17:46:56 2008

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