8bsk

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[8bsk]] 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=8BSK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BSK FirstGlance]. <br>
<table><tr><td colspan='2'>[[8bsk]] 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=8BSK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BSK FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=04A:N,N-[SULFANEDIYLBIS(ETHANE-2,1-DIYL-1,3,4-THIADIAZOLE-5,2-DIYL)]BIS(2-PHENYLACETAMIDE)'>04A</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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]] 2.1&#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=04A:N,N-[SULFANEDIYLBIS(ETHANE-2,1-DIYL-1,3,4-THIADIAZOLE-5,2-DIYL)]BIS(2-PHENYLACETAMIDE)'>04A</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=8bsk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bsk OCA], [https://pdbe.org/8bsk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bsk RCSB], [https://www.ebi.ac.uk/pdbsum/8bsk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bsk ProSAT]</span></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=8bsk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bsk OCA], [https://pdbe.org/8bsk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bsk RCSB], [https://www.ebi.ac.uk/pdbsum/8bsk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bsk ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/GLSK_HUMAN GLSK_HUMAN] Catalyzes the first reaction in the primary pathway for the renal catabolism of glutamine. Plays a role in maintaining acid-base homeostasis. Regulates the levels of the neurotransmitter glutamate in the brain. Isoform 2 lacks catalytic activity.
[https://www.uniprot.org/uniprot/GLSK_HUMAN GLSK_HUMAN] Catalyzes the first reaction in the primary pathway for the renal catabolism of glutamine. Plays a role in maintaining acid-base homeostasis. Regulates the levels of the neurotransmitter glutamate in the brain. Isoform 2 lacks catalytic activity.
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Tumors have evolved a variety of methods to reprogram conventional metabolic pathways to favor their own nutritional needs, including glutaminolysis, the first step of which is the hydrolysis of glutamine to glutamate by the amidohydrolase glutaminase 1 (GLS1). A GLS1 inhibitor could potentially target certain cancers by blocking the tumor cell's ability to produce glutamine-derived nutrients. Starting from the known GLS1 inhibitor bis-2-(5-phenylacetamido-1,2,4-thiadiazol-2-yl)ethyl sulfide, we describe the medicinal chemistry evolution of a series from lipophilic inhibitors with suboptimal physicochemical and pharmacokinetic properties to cell potent examples with reduced molecular weight and lipophilicity, leading to compounds with greatly improved oral exposure that demonstrate in vivo target engagement accompanied by activity in relevant disease models.
 
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Discovery of a Thiadiazole-Pyridazine-Based Allosteric Glutaminase 1 Inhibitor Series That Demonstrates Oral Bioavailability and Activity in Tumor Xenograft Models.,Finlay MRV, Anderton M, Bailey A, Boyd S, Brookfield J, Cairnduff C, Charles M, Cheasty A, Critchlow SE, Culshaw J, Ekwuru T, Hollingsworth I, Jones N, Leroux F, Littleson M, McCarron H, McKelvie J, Mooney L, Nissink JWM, Perkins D, Powell S, Quesada MJ, Raubo P, Sabin V, Smith J, Smith PD, Stark A, Ting A, Wang P, Wilson Z, Winter-Holt JJ, Wood JM, Wrigley GL, Yu G, Zhang P J Med Chem. 2019 Jul 25;62(14):6540-6560. doi: 10.1021/acs.jmedchem.9b00260. Epub , 2019 Jul 16. PMID:31199640<ref>PMID:31199640</ref>
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==See Also==
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*[[Glutaminase 3D structures|Glutaminase 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 8bsk" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Human GLS in complex with compound 3

PDB ID 8bsk

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