1t7x
From Proteopedia
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- | [[Image:1t7x.jpg|left|200px]] | + | [[Image:1t7x.jpg|left|200px]] |
- | + | ||
- | '''Zn-alpha-2-glycoprotein; refolded CHO-ZAG PEG 400''' | + | {{Structure |
+ | |PDB= 1t7x |SIZE=350|CAPTION= <scene name='initialview01'>1t7x</scene>, resolution 3.10Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= AZGP1, ZAG, ZNGP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
+ | }} | ||
+ | |||
+ | '''Zn-alpha-2-glycoprotein; refolded CHO-ZAG PEG 400''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1T7X is a [ | + | 1T7X is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T7X OCA]. |
==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:// | + | 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] |
[[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]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:14:59 2008'' |
Revision as of 12:15, 20 March 2008
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, resolution 3.10Å | |||||||
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Ligands: | |||||||
Gene: | AZGP1, ZAG, ZNGP1 (Homo sapiens) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Zn-alpha-2-glycoprotein; refolded CHO-ZAG PEG 400
Overview
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.
About this Structure
1T7X 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
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