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==Macaca mulatta galectin-10/Charcot-Leyden crystal protein== | |||
<StructureSection load='7xxx' size='340' side='right'caption='[[7xxx]], [[Resolution|resolution]] 1.94Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7xxx]] 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=7XXX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XXX FirstGlance]. <br> | |||
</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=7xxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xxx OCA], [https://pdbe.org/7xxx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xxx RCSB], [https://www.ebi.ac.uk/pdbsum/7xxx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xxx 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 7xxx" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Macaca mulatta]] | |||
[[Category: Su JY]] | |||
Revision as of 23:28, 12 April 2023
Macaca mulatta galectin-10/Charcot-Leyden crystal proteinMacaca mulatta galectin-10/Charcot-Leyden crystal protein
Structural highlights
Publication Abstract from PubMedCharcot-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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