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6l64
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==X-ray structure of human galectin-10 in complex with D-glucose== | |
| + | <StructureSection load='6l64' size='340' side='right'caption='[[6l64]], [[Resolution|resolution]] 2.08Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6l64]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L64 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6L64 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6l64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l64 OCA], [http://pdbe.org/6l64 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6l64 RCSB], [http://www.ebi.ac.uk/pdbsum/6l64 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6l64 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/LEG10_HUMAN LEG10_HUMAN]] Regulates immune responses through the recognition of cell-surface glycans. Essential for the anergy and suppressive function of CD25-positive regulatory T-cells (Treg).<ref>PMID:17502455</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The galectins are a family of beta-galactoside-specific animal lectins, and have attracted much attention as novel regulators of the immune system. Galectin-10 is well-expressed in eosinophils, and spontaneously forms Charcot-Leyden crystals (CLCs), during prolonged eosinophilic inflammatory reactions, which are frequently observed in eosinophilic diseases. Although biochemical and structural characterizations of galectin-10 have been done, its biological role and molecular mechanism are still unclear, and few X-ray structures of galectin-10 in complex with monosaccharides/oligosaccharides have been reported. Here, X-ray structures of galectin-10 in complexes with seven monosaccharides are presented with biochemical analyses to detect interactions of galectin-10 with monosaccharides/oligosaccharides. Galectin-10 forms a homo-dimer in the face-to-face orientation, and the monosaccharides bind to the carbohydrate recognition site composed of amino acid residues from two galectin-10 molecules of dimers, suggesting that galectin-10 dimer likely captures the monosaccharides in solution and in vivo. d-Glucose, d-allose, d-arabinose, and D-N-acetylgalactosamine bind to the interfaces between galectin-10 dimers in crystals, and they affect the stability of molecular packing in crystals, leading to easy-dissolving of CLCs, and/or inhibiting the formation of CLCs. These monosaccharides may serve as effectors of G10 to form CLCs in vivo. | ||
| - | + | Structures of human galectin-10/monosaccharide complexes demonstrate potential of monosaccharides as effectors in forming Charcot-Leyden crystals.,Itoh A, Nonaka Y, Nakakita SI, Yoshida H, Nishi N, Nakamura T, Kamitori S Biochem Biophys Res Commun. 2020 Feb 17. pii: S0006-291X(20)30303-X. doi:, 10.1016/j.bbrc.2020.02.037. PMID:32081418<ref>PMID:32081418</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6l64" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Kamitori, S]] | [[Category: Kamitori, S]] | ||
| + | [[Category: Beta-sandwich structure]] | ||
| + | [[Category: Lectin]] | ||
| + | [[Category: Sugar binding protein]] | ||
Revision as of 06:41, 4 March 2020
X-ray structure of human galectin-10 in complex with D-glucose
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