3x29

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

spinqualitylabelsall models 3x29, resolution 3.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3x29 is a 4 chain structure with sequence from Clostridium perfringens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.7Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ELTB_CLOPF This enterotoxin is responsible for many cases of a mild type of food poisoning. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA