9uo6: Difference between revisions

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'''Unreleased structure'''


The entry 9uo6 is ON HOLD  until Paper Publication
==Cryo-EM structure of the Xenopus IgX-Fc hexamer==
<StructureSection load='9uo6' size='340' side='right'caption='[[9uo6]], [[Resolution|resolution]] 3.29&Aring;' 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]] 3.29&#8491;</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.


Authors:  
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>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</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]]
Retrieved from "https://proteopedia.org/9uo6"