3dgq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "3dgq" [edit=sysop:move=sysop])
Current revision (15:09, 1 November 2023) (edit) (undo)
 
(5 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:3dgq.png|left|200px]]
 
-
{{STRUCTURE_3dgq| PDB=3dgq | SCENE= }}
+
==Crystal structure of the glutathione transferase PI enzyme in complex with the bifunctional inhibitor, etharapta==
 +
<StructureSection load='3dgq' size='340' side='right'caption='[[3dgq]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[3dgq]] is a 2 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=3DGQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DGQ FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EAA:ETHACRYNIC+ACID'>EAA</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=3dgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dgq OCA], [https://pdbe.org/3dgq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dgq RCSB], [https://www.ebi.ac.uk/pdbsum/3dgq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dgq ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/GSTP1_HUMAN GSTP1_HUMAN] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration.<ref>PMID:21668448</ref>
 +
== 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/dg/3dgq_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3dgq ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Double trouble: A hybrid organic-inorganic (organometallic) inhibitor was designed to target glutathione transferases. The metal center is used to direct protein binding, while the organic moiety acts as the active-site inhibitor (see picture). The mechanism of inhibition was studied using a range of biophysical and biochemical methods.
-
===Crystal structure of the glutathione transferase PI enzyme in complex with the bifunctional inhibitor, etharapta===
+
Rational design of an organometallic glutathione transferase inhibitor.,Ang WH, Parker LJ, De Luca A, Juillerat-Jeanneret L, Morton CJ, Lo Bello M, Parker MW, Dyson PJ Angew Chem Int Ed Engl. 2009;48(21):3854-7. PMID:19396894<ref>PMID:19396894</ref>
-
{{ABSTRACT_PUBMED_19396894}}
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
==About this Structure==
+
<div class="pdbe-citations 3dgq" style="background-color:#fffaf0;"></div>
-
[[3dgq]] is a 2 chain structure with 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=3DGQ OCA].
+
==See Also==
==See Also==
-
*[[Glutathione S-transferase|Glutathione S-transferase]]
+
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<ref group="xtra">PMID:019396894</ref><references group="xtra"/>
+
__TOC__
-
[[Category: Glutathione transferase]]
+
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Parker, L J.]]
+
[[Category: Large Structures]]
-
[[Category: Detoxification]]
+
[[Category: Parker LJ]]
-
[[Category: Ethacrynic-acid]]
+
-
[[Category: Etharapta]]
+
-
[[Category: Glutathione]]
+
-
[[Category: Ruthenium]]
+
-
[[Category: Transferase]]
+

Current revision

Crystal structure of the glutathione transferase PI enzyme in complex with the bifunctional inhibitor, etharapta

PDB ID 3dgq

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3dgq"
Personal tools