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7xxz
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 7xxz is ON HOLD Authors: Su, J.Y. Description: Macaca mulatta galectin-10/Charcot-Leyden crystal protein with glycerol [[Category: Unreleased Struc...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Macaca mulatta galectin-10/Charcot-Leyden crystal protein with glycerol== | |
| + | <StructureSection load='7xxz' size='340' side='right'caption='[[7xxz]], [[Resolution|resolution]] 1.83Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7xxz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Macaca_mulatta Macaca mulatta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XXZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XXZ 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]] 1.83Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=7xxz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xxz OCA], [https://pdbe.org/7xxz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xxz RCSB], [https://www.ebi.ac.uk/pdbsum/7xxz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xxz ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Charcot-Leyden crystals (CLCs) are the hallmark of many eosinophilic-based diseases, such as asthma. Here, we report that reduced glutathione (GSH) disrupts CLCs and inhibits crystallization of human galectin-10 (Gal-10). GSH has no effect on CLCs from monkeys ( Macaca fascicularis or M. mulatta), even though monkey Gal-10s contain Cys29 and Cys32. Interestingly, human Gal-10 contains another cysteine residue (Cys57). Because GSH cannot disrupt CLCs formed by the human Gal-10 variant C57A or inhibit its crystallization, the effects of GSH on human Gal-10 or CLCs most likely occur by chemical modification of Cys57. We further report the crystal structures of Gal-10 from M. fascicularis and M. mulatta, along with their ability to bind to lactose and inhibit erythrocyte agglutination. Structural comparison with human Gal-10 shows that Cys57 and Gln75 within the ligand binding site are responsible for the loss of lactose binding. Pull-down experiments and mass spectrometry show that human Gal-10 interacts with tubulin alpha-1B, with GSH, GTP and Mg (2+) stabilizing this interaction and colchicine inhibiting it. Overall, this study enhances our understanding of Gal-10 function and CLC formation and suggests that GSH may be used as a pharmaceutical agent to ameliorate CLC-induced diseases. | ||
| - | + | Glutathione disrupts galectin-10 Charcot-Leyden crystal formation to possibly ameliorate eosinophil-based diseases such as asthma.,Na H, Sayed H, Ayala GJ, Wang X, Liu Y, Yu J, Liu T, Mayo KH, Su J Acta Biochim Biophys Sin (Shanghai). 2023 Mar 25. doi: 10.3724/abbs.2023050. PMID:36988350<ref>PMID:36988350</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Su | + | <div class="pdbe-citations 7xxz" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Macaca mulatta]] | ||
| + | [[Category: Su JY]] | ||
Current revision
Macaca mulatta galectin-10/Charcot-Leyden crystal protein with glycerol
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