3X29

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

3X29 の概要

• エントリーDOI: 10.2210/pdb3x29/pdb
• 分子名称: Claudin-19, Heat-labile enterotoxin B chain (2 entities in total)
• 機能のキーワード: toxin-cell adhesion complex, tight junction, cell adhesion, enterotoxin, membrane protein, receptor binding
• 由来する生物種: Mus musculus (mouse); 詳細
• 細胞内の位置: Cell junction, tight junction: Q9ET38
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 65094.18

構造登録者

Saitoh, Y.,Suzuki, H.,Tani, K.,Nishikawa, K.,Irie, K.,Ogura, Y.,Tamura, A.,Tsukita, S.,Fujiyoshi, Y. (登録日: 2014-12-13, 公開日: 2015-01-21, 最終更新日: 2024-10-16)

主引用文献

Saitoh, Y.,Suzuki, H.,Tani, K.,Nishikawa, K.,Irie, K.,Ogura, Y.,Tamura, A.,Tsukita, S.,Fujiyoshi, Y.
Structural insight into tight junction disassembly by Clostridium perfringens enterotoxin
Science, 347:775-778, 2015

PubMed Abstract: 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 Å 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.

PubMed: 25678664
DOI: 10.1126/science.1261833

実験手法

X-RAY DIFFRACTION (3.7 Å)