3X29
CRYSTAL STRUCTURE of MOUSE CLAUDIN-19 IN COMPLEX with C-TERMINAL FRAGMENT OF CLOSTRIDIUM PERFRINGENS ENTEROTOXIN
Summary for 3X29
| Entry DOI | 10.2210/pdb3x29/pdb |
| Descriptor | Claudin-19, Heat-labile enterotoxin B chain (2 entities in total) |
| Functional Keywords | toxin-cell adhesion complex, tight junction, cell adhesion, enterotoxin, membrane protein, receptor binding |
| Biological source | Mus musculus (mouse) More |
| Cellular location | Cell junction, tight junction: Q9ET38 |
| Total number of polymer chains | 4 |
| Total formula weight | 65094.18 |
| Authors | Saitoh, Y.,Suzuki, H.,Tani, K.,Nishikawa, K.,Irie, K.,Ogura, Y.,Tamura, A.,Tsukita, S.,Fujiyoshi, Y. (deposition date: 2014-12-13, release date: 2015-01-21, Last modification date: 2024-10-16) |
| Primary citation | 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 Cited by 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: 25678664DOI: 10.1126/science.1261833 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.7 Å) |
Structure validation
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