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9uo6
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure of the Xenopus IgX-Fc hexamer== | |
| + | <StructureSection load='9uo6' size='340' side='right'caption='[[9uo6]], [[Resolution|resolution]] 3.29Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9uo6]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9UO6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9UO6 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.29Å</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=9uo6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9uo6 OCA], [https://pdbe.org/9uo6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9uo6 RCSB], [https://www.ebi.ac.uk/pdbsum/9uo6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9uo6 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q6INK3_XENLA Q6INK3_XENLA] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Polymeric immunoglobulins are essential components of the immune system in jawed vertebrates. While mammalian immunoglobulin M (IgM) typically forms a pentamer linked by the joining chain (J-chain), Xenopus laevis IgX can assemble into a J-chain-independent polymer. Here, we present the cryo-electron microscopy (cryo-EM) structure of IgX, revealing its hexameric configuration. By incorporating the IgX tailpiece into human IgM, we achieved efficient IgM hexamer formation. Truncating IgM's natural tailpiece to a range of 11 to 16 residues also substantially enhanced hexamerization efficiency. Furthermore, introducing a shortened IgM tailpiece to IgG resulted in effective IgG hexamer formation. We further show that the engineered IgM and IgG hexamers targeting CD20 demonstrated robust complement-dependent cytotoxicity (CDC) against several B lymphoma cells. In addition, the IgG-Fc hexamer functioned as a decoy, attenuating CDC in cell cultures. These findings deepen our understanding of polymeric immunoglobulin evolution and introduce innovative strategies for the development of IgM- and IgG-based biologics. | ||
| - | + | Xenopus IgX informs engineering strategies of IgM and IgG hexamers.,Zhang R, Ji C, Li S, Li N, Gao N, Xiao J Sci Adv. 2025 Nov 7;11(45):eaea3737. doi: 10.1126/sciadv.aea3737. Epub 2025 Nov , 5. PMID:41191733<ref>PMID:41191733</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 9uo6" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Xenopus laevis]] | ||
| + | [[Category: Ji C]] | ||
| + | [[Category: Xiao J]] | ||
| + | [[Category: Zhang R]] | ||
Current revision
Cryo-EM structure of the Xenopus IgX-Fc hexamer
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