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1t7v

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[[Image:1t7v.jpg|left|200px]]
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{{Seed}}
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[[Image:1t7v.png|left|200px]]
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{{STRUCTURE_1t7v| PDB=1t7v | SCENE= }}
{{STRUCTURE_1t7v| PDB=1t7v | SCENE= }}
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'''Zn-alpha-2-glycoprotein; baculo-ZAG PEG 200'''
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===Zn-alpha-2-glycoprotein; baculo-ZAG PEG 200===
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==Overview==
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Zn-alpha2-glycoprotein (ZAG) is a 41 kDa soluble protein that is present in most bodily fluids. The previously reported 2.8 A crystal structure of ZAG isolated from human serum demonstrated the structural similarity between ZAG and class I major histocompatibility complex (MHC) molecules and revealed a non-peptidic ligand in the ZAG counterpart of the MHC peptide-binding groove. Here we present crystallographic studies to explore further the nature of the non-peptidic ligand in the ZAG groove. Comparison of the structures of several forms of recombinant ZAG, including a 1.95 A structure derived from ZAG expressed in insect cells, suggests that the non-peptidic ligand in the current structures and in the structure of serum ZAG is a polyethylene glycol (PEG), which is present in the crystallization conditions used. Further support for PEG binding in the ZAG groove is provided by the finding that PEG displaces a fluorophore-tagged fatty acid from the ZAG binding site. From these results we hypothesize that our purified forms of ZAG do not contain a bound endogenous ligand, but that the ZAG groove is capable of binding hydrophobic molecules, which may relate to its function.
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The line below this paragraph, {{ABSTRACT_PUBMED_15477100}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15477100 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15477100}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Crystallographic studies of ligand binding by Zn-alpha2-glycoprotein., Delker SL, West AP Jr, McDermott L, Kennedy MW, Bjorkman PJ, J Struct Biol. 2004 Nov;148(2):205-13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15477100 15477100]
Crystallographic studies of ligand binding by Zn-alpha2-glycoprotein., Delker SL, West AP Jr, McDermott L, Kennedy MW, Bjorkman PJ, J Struct Biol. 2004 Nov;148(2):205-13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15477100 15477100]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10206894 10206894]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Mhc class i homolog]]
[[Category: Mhc class i homolog]]
[[Category: Peg]]
[[Category: Peg]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:38:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:56:30 2008''

Revision as of 12:56, 28 July 2008

Image:1t7v.png

Template:STRUCTURE 1t7v

Zn-alpha-2-glycoprotein; baculo-ZAG PEG 200

Template:ABSTRACT PUBMED 15477100

About this Structure

1T7V is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystallographic studies of ligand binding by Zn-alpha2-glycoprotein., Delker SL, West AP Jr, McDermott L, Kennedy MW, Bjorkman PJ, J Struct Biol. 2004 Nov;148(2):205-13. PMID:15477100

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 15:56:30 2008

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