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1t7y

From Proteopedia

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Current revision

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

Structural highlights

1t7y is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.8Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ZA2G_HUMAN Stimulates lipid degradation in adipocytes and causes the extensive fat losses associated with some advanced cancers. May bind polyunsaturated fatty acids.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Delker SL, West AP Jr, McDermott L, Kennedy MW, Bjorkman PJ. Crystallographic studies of ligand binding by Zn-alpha2-glycoprotein. J Struct Biol. 2004 Nov;148(2):205-13. PMID:15477100 doi:10.1016/j.jsb.2004.04.009

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1t7y"

@@ Line 1: / Line 1: @@
 ==Zn-alpha-2-glycoprotein; baculo-ZAG PEG 200, no glycerol==
-<StructureSection load='1t7y' size='340' side='right' caption='[[1t7y]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+<StructureSection load='1t7y' size='340' side='right'caption='[[1t7y]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1t7y]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T7Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1T7Y FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1t7y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T7Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T7Y FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zag|1zag]], [[1t7v|1t7v]], [[1t7w|1t7w]], [[1t7x|1t7x]], [[1t7z|1t7z]], [[1t80|1t80]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AZGP1, ZAG, ZNGP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1t7y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t7y OCA], [https://pdbe.org/1t7y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t7y RCSB], [https://www.ebi.ac.uk/pdbsum/1t7y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t7y ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t7y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t7y OCA], [http://pdbe.org/1t7y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1t7y RCSB], [http://www.ebi.ac.uk/pdbsum/1t7y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1t7y ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ZA2G_HUMAN ZA2G_HUMAN]] Stimulates lipid degradation in adipocytes and causes the extensive fat losses associated with some advanced cancers. May bind polyunsaturated fatty acids.
+[https://www.uniprot.org/uniprot/ZA2G_HUMAN ZA2G_HUMAN] Stimulates lipid degradation in adipocytes and causes the extensive fat losses associated with some advanced cancers. May bind polyunsaturated fatty acids.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t7/1t7y_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t7/1t7y_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 34: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Bjorkman, P J]]
+[[Category: Large Structures]]
-[[Category: Delker, S L]]
+[[Category: Bjorkman PJ]]
-[[Category: Kennedy, M W]]
+[[Category: Delker SL]]
-[[Category: McDermott, L]]
+[[Category: Kennedy MW]]
-[[Category: West, A P]]
+[[Category: McDermott L]]
-[[Category: Lipid binding protein]]
+[[Category: West Jr AP]]
-[[Category: Mhc class i homolog]]

1t7y

From Proteopedia

Current revision

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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