6akg
From Proteopedia
Crystal structure of mouse claudin-3 P134G mutant in complex with C-terminal fragment of Clostridium perfringens enterotoxin
Structural highlights
FunctionCLD3_MOUSE Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.[1] Publication Abstract from PubMedTight 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 A 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. Morphologic determinant of tight junctions revealed by claudin-3 structures.,Nakamura S, Irie K, Tanaka H, Nishikawa K, Suzuki H, Saitoh Y, Tamura A, Tsukita S, Fujiyoshi Y Nat Commun. 2019 Feb 18;10(1):816. doi: 10.1038/s41467-019-08760-7. PMID:30778075[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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