6ov2

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'''Unreleased structure'''
 
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The entry 6ov2 is ON HOLD until Paper Publication
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==Crystal structure of human claudin-9 in complex with Clostridium perfringens entertoxin C-terminal domain in closed form==
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<StructureSection load='6ov2' size='340' side='right'caption='[[6ov2]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6ov2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OV2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OV2 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6ov2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ov2 OCA], [https://pdbe.org/6ov2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ov2 RCSB], [https://www.ebi.ac.uk/pdbsum/6ov2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ov2 ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The human pathogenic bacterium Clostridium perfringens secretes an enterotoxin (CpE) that targets claudins through its C-terminal receptor-binding domain (cCpE). Isoform-specific binding by CpE causes dissociation of claudins and tight junctions (TJs), resulting in cytotoxicity and breakdown of the gut epithelial barrier. Here, we present crystal structures of human claudin-9 (hCLDN-9) in complex with cCpE at 3.2 and 3.3 A. We show that hCLDN-9 is a high-affinity CpE receptor and that hCLDN-9-expressing cells undergo cell death when treated with CpE but not cCpE, which lacks its cytotoxic domain. Structures reveal cCpE-induced alterations to 2 epitopes known to enable claudin self-assembly and expose high-affinity interactions between hCLDN-9 and cCpE that explain isoform-specific recognition. These findings elucidate the molecular bases for hCLDN-9 selective ion permeability and binding by CpE, and provide mechanisms for how CpE disrupts gut homeostasis by dissociating claudins and TJs to affect epithelial adhesion and intercellular transport.
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Authors:
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Claudin-9 structures reveal mechanism for toxin-induced gut barrier breakdown.,Vecchio AJ, Stroud RM Proc Natl Acad Sci U S A. 2019 Sep 3;116(36):17817-17824. doi:, 10.1073/pnas.1908929116. Epub 2019 Aug 21. PMID:31434788<ref>PMID:31434788</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6ov2" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Clostridium perfringens]]
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Stroud RM]]
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[[Category: Vecchio AJ]]

Current revision

Crystal structure of human claudin-9 in complex with Clostridium perfringens entertoxin C-terminal domain in closed form

PDB ID 6ov2

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