6AKG

Crystal structure of mouse claudin-3 P134G mutant in complex with C-terminal fragment of Clostridium perfringens enterotoxin

Summary for 6AKG

• Entry DOI: 10.2210/pdb6akg/pdb
• Related: 6AKE 6AKF
• Descriptor: Claudin-3, Heat-labile enterotoxin B chain (2 entities in total)
• Functional Keywords: cell adhesion, tight junction, membrane protein-toxin complex, membrane protein/toxin
• Biological source: Mus musculus (Mouse); More
• Total number of polymer chains: 4
• Total formula weight: 66392.54

Authors

Nakamura, S.,Irie, K.,Fujiyoshi, Y. (deposition date: 2018-08-31, release date: 2019-02-20, Last modification date: 2024-10-23)

Primary citation

Nakamura, S.,Irie, K.,Tanaka, H.,Nishikawa, K.,Suzuki, H.,Saitoh, Y.,Tamura, A.,Tsukita, S.,Fujiyoshi, Y.
Morphologic determinant of tight junctions revealed by claudin-3 structures.
Nat Commun, 10:816-816, 2019

PubMed Abstract: Tight junction is a cell adhesion apparatus functioning as barrier and/or channel in the paracellular spaces of epithelia. Claudin is the major component of tight junction and polymerizes to form tight junction strands with various morphologies that may correlate with their functions. Here we present the crystal structure of mammalian claudin-3 at 3.6 Å resolution. The third transmembrane helix of claudin-3 is clearly bent compared with that of other subtypes. Structural analysis of additional two mutants with a single mutation representing other subtypes in the third helix indicates that this helix takes a bent or straight structure depending on the residue. The presence or absence of the helix bending changes the positions of residues related to claudin-claudin interactions and affects the morphology and adhesiveness of the tight junction strands. These results evoke a model for tight junction strand formation with different morphologies - straight or curvy strands - observed in native epithelia.

PubMed: 30778075
DOI: 10.1038/s41467-019-08760-7

Experimental method

X-RAY DIFFRACTION (4.3 Å)