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1tu8

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[[Image:1tu8.gif|left|200px]]
 
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==STructure of Onchoverca volvulus Pi-class Glutathione S-transferase with its kompetitive inhibitor s-hexyl-GSH==
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The line below this paragraph, containing "STRUCTURE_1tu8", creates the "Structure Box" on the page.
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<StructureSection load='1tu8' size='340' side='right'caption='[[1tu8]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1tu8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Onchocerca_volvulus Onchocerca volvulus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TU8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TU8 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTX:S-HEXYLGLUTATHIONE'>GTX</scene></td></tr>
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{{STRUCTURE_1tu8| PDB=1tu8 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tu8 OCA], [https://pdbe.org/1tu8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tu8 RCSB], [https://www.ebi.ac.uk/pdbsum/1tu8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tu8 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GSTP_ONCVO GSTP_ONCVO] Appears to play a central role in the parasite detoxification system.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tu/1tu8_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1tu8 ConSurf].
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<div style="clear:both"></div>
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'''STructure of Onchoverca volvulus Pi-class Glutathione S-transferase with its kompetitive inhibitor s-hexyl-GSH'''
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==See Also==
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*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Onchocerciasis is a debilitating parasitic disease caused by the filarial worm Onchocerca volvulus. Similar to other helminth parasites, O. volvulus is capable of evading the host's immune responses by a variety of defense mechanisms, including the detoxification activities of the glutathione S-transferases (GSTs). Additionally, in response to drug treatment, helminth GSTs are highly up-regulated, making them tempting targets both for chemotherapy and for vaccine development. We analyzed the three-dimensional x-ray structure of the major cytosolic GST from O. volvulus (Ov-GST2) in complex with its natural substrate glutathione and its competitive inhibitor S-hexylglutathione at 1.5 and 1.8 angstrom resolution, respectively. From the perspective of the biochemical classification, the Ov-GST2 seems to be related to pi-class GSTs. However, in comparison to other pi-class GSTs, in particular to the host's counterpart, the Ov-GST2 reveals significant and unusual differences in the sequence and overall structure. Major differences can be found in helix alpha-2, an important region for substrate recognition. Moreover, the binding site for the electrophilic co-substrate is spatially increased and more solvent-accessible. These structural alterations are responsible for different substrate specificities and will form the basis of parasite-specific structure-based drug design investigations.
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[[Category: Large Structures]]
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==About this Structure==
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1TU8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Onchocerca_volvulus Onchocerca volvulus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TU8 OCA].
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==Reference==
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Structure of the major cytosolic glutathione S-transferase from the parasitic nematode Onchocerca volvulus., Perbandt M, Hoppner J, Betzel C, Walter RD, Liebau E, J Biol Chem. 2005 Apr 1;280(13):12630-6. Epub 2005 Jan 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15640152 15640152]
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[[Category: Glutathione transferase]]
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[[Category: Onchocerca volvulus]]
[[Category: Onchocerca volvulus]]
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[[Category: Single protein]]
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[[Category: Perbandt M]]
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[[Category: Perbandt, M.]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:22:18 2008''
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Current revision

STructure of Onchoverca volvulus Pi-class Glutathione S-transferase with its kompetitive inhibitor s-hexyl-GSH

PDB ID 1tu8

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