3x29

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== Function ==
== Function ==
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[https://www.uniprot.org/uniprot/CLD19_MOUSE CLD19_MOUSE] Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
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[https://www.uniprot.org/uniprot/ELTB_CLOPF ELTB_CLOPF] This enterotoxin is responsible for many cases of a mild type of food poisoning.
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== Publication Abstract from PubMed ==
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The C-terminal region of Clostridium perfringens enterotoxin (C-CPE) can bind to specific claudins, resulting in the disintegration of tight junctions (TJs) and an increase in the paracellular permeability across epithelial cell sheets. Here we present the structure of mammalian claudin-19 in complex with C-CPE at 3.7 A resolution. The structure shows that C-CPE forms extensive hydrophobic and hydrophilic interactions with the two extracellular segments of claudin-19. The claudin-19/C-CPE complex shows no density of a short extracellular helix that is critical for claudins to assemble into TJ strands. The helix displacement may thus underlie C-CPE-mediated disassembly of TJs.
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Tight junctions. Structural insight into tight junction disassembly by Clostridium perfringens enterotoxin.,Saitoh Y, Suzuki H, Tani K, Nishikawa K, Irie K, Ogura Y, Tamura A, Tsukita S, Fujiyoshi Y Science. 2015 Feb 13;347(6223):775-8. doi: 10.1126/science.1261833. PMID:25678664<ref>PMID:25678664</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
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Current revision

CRYSTAL STRUCTURE of MOUSE CLAUDIN-19 IN COMPLEX with C-TERMINAL FRAGMENT OF CLOSTRIDIUM PERFRINGENS ENTEROTOXIN

PDB ID 3x29

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