3x29
From Proteopedia
CRYSTAL STRUCTURE of MOUSE CLAUDIN-19 IN COMPLEX with C-TERMINAL FRAGMENT OF CLOSTRIDIUM PERFRINGENS ENTEROTOXIN
Structural highlights
FunctionELTB_CLOPF This enterotoxin is responsible for many cases of a mild type of food poisoning. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. Loading citation details.. Citations No citations found References
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Categories: Clostridium perfringens | Large Structures | Mus musculus | Fujiyoshi Y | Irie K | Nishikawa K | Ogura Y | Saitoh Y | Suzuki H | Tamura A | Tani K | Tsukita S
