6ov2: Difference between revisions
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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> | <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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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Latest revision as of 11:12, 17 October 2024
Crystal structure of human claudin-9 in complex with Clostridium perfringens entertoxin C-terminal domain in closed formCrystal structure of human claudin-9 in complex with Clostridium perfringens entertoxin C-terminal domain in closed form
Structural highlights
Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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