1t7y

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(New page: 200px<br /> <applet load="1t7y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t7y, resolution 2.80&Aring;" /> '''Zn-alpha-2-glycopro...)
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[[Image:1t7y.gif|left|200px]]<br />
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[[Image:1t7y.gif|left|200px]]<br /><applet load="1t7y" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1t7y" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1t7y, resolution 2.80&Aring;" />
caption="1t7y, resolution 2.80&Aring;" />
'''Zn-alpha-2-glycoprotein; baculo-ZAG PEG 200, no glycerol'''<br />
'''Zn-alpha-2-glycoprotein; baculo-ZAG PEG 200, no glycerol'''<br />
==Overview==
==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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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==
==About this Structure==
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1T7Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1T7Y OCA].
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1T7Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T7Y OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Bjorkman, P.J.]]
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[[Category: Bjorkman, P J.]]
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[[Category: Delker, S.L.]]
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[[Category: Delker, S L.]]
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[[Category: Jr., A.P.West.]]
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[[Category: Jr., A P.West.]]
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[[Category: Kennedy, M.W.]]
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[[Category: Kennedy, M W.]]
[[Category: McDermott, L.]]
[[Category: McDermott, L.]]
[[Category: NAG]]
[[Category: NAG]]
[[Category: mhc class i homolog]]
[[Category: mhc class i homolog]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:21:44 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:10:52 2008''

Revision as of 13:10, 21 February 2008


1t7y, resolution 2.80Å

Drag the structure with the mouse to rotate

Zn-alpha-2-glycoprotein; baculo-ZAG PEG 200, no glycerol

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

1T7Y is a Single protein structure of sequence from Homo sapiens with as ligand. 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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