5yvo: Difference between revisions

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New page: '''Unreleased structure''' The entry 5yvo is ON HOLD Authors: Saisawang, C., Ketterman, A., Wongsantichon, J. Description: Human Glutathione Transferase Omega1 covalently bound to ML17...
 
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'''Unreleased structure'''


The entry 5yvo is ON HOLD
==Human Glutathione Transferase Omega1 covalently bound to ML175 inhibitor==
<StructureSection load='5yvo' size='340' side='right'caption='[[5yvo]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5yvo]] 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=5YVO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YVO 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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MLX:~{N}-[3-[2-chloranylethanoyl-(4-nitrophenyl)amino]propyl]-2,2,2-tris(fluoranyl)ethanamide'>MLX</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=5yvo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yvo OCA], [https://pdbe.org/5yvo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yvo RCSB], [https://www.ebi.ac.uk/pdbsum/5yvo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yvo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GSTO1_HUMAN GSTO1_HUMAN] Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. Has S-(phenacyl)glutathione reductase activity. Has also glutathione S-transferase activity. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid.<ref>PMID:10783391</ref> <ref>PMID:11511179</ref> <ref>PMID:17226937</ref> <ref>PMID:18028863</ref> <ref>PMID:21106529</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In the human neuroblastoma SH-SY5Y cell line, the glutathione transferase Omega 1-1 (GSTO1-1) appears to modulate Akt and MEK1/2 kinase activation. We observed a glutathionylation modification was involved in the activation of Akt but not MEK1/2. With the specific GSTO1-1 inhibitor ML175, we show the enzyme activity of GSTO1-1 is important for modulation as the inhibited GSTO1-1 allowed activation of both Akt and MEK1/2. The inhibition of GSTO1-1 showed a similar extent of activation of Akt and MEK1/2 as treatment by the endotoxin lipopolysaccharide. The GSTO1-1 also either directly interacts with Akt and MEK1/2 or interacts with a protein complexed with Akt and MEK1/2 as both kinases coimmunoprecipitated with GSTO1-1. The results suggest that GSTO1-1 enzyme activity inhibits the activation of these two kinases to maintain basal levels. The possible regulation by GSTO1-1 is of interest as both kinases have hundreds of potential downstream targets that are known to have contributions to various cellular processes including survival, growth, proliferation, and metabolism.


Authors: Saisawang, C., Ketterman, A., Wongsantichon, J.
Glutathione transferase Omega 1-1 (GSTO1-1) modulates Akt and MEK1/2 signaling in human neuroblastoma cell SH-SY5Y.,Saisawang C, Wongsantichon J, Robinson RC, Ketterman AJ Proteins. 2019 Jul;87(7):588-595. doi: 10.1002/prot.25683. Epub 2019 Mar 25. PMID:30874320<ref>PMID:30874320</ref>


Description: Human Glutathione Transferase Omega1 covalently bound to ML175 inhibitor
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Wongsantichon, J]]
<div class="pdbe-citations 5yvo" style="background-color:#fffaf0;"></div>
[[Category: Saisawang, C]]
 
[[Category: Ketterman, A]]
==See Also==
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Ketterman A]]
[[Category: Saisawang C]]
[[Category: Wongsantichon J]]