4P79
Crystal structure of mouse claudin-15
Summary for 4P79
| Entry DOI | 10.2210/pdb4p79/pdb |
| Descriptor | Claudin-15, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate (3 entities in total) |
| Functional Keywords | cell adhesion, tight junction, membrane protein, paracellular channel |
| Biological source | Mus musculus (Mouse) |
| Cellular location | Cell junction, tight junction: Q9Z0S5 |
| Total number of polymer chains | 1 |
| Total formula weight | 22157.74 |
| Authors | Suzuki, H.,Nishizawa, T.,Tani, K.,Yamazaki, Y.,Tamura, A.,Ishitani, R.,Dohmae, N.,Tsukita, S.,Nureki, O.,Fujiyoshi, Y. (deposition date: 2014-03-26, release date: 2014-04-30, Last modification date: 2024-11-20) |
| Primary citation | Suzuki, H.,Nishizawa, T.,Tani, K.,Yamazaki, Y.,Tamura, A.,Ishitani, R.,Dohmae, N.,Tsukita, S.,Nureki, O.,Fujiyoshi, Y. Crystal structure of a claudin provides insight into the architecture of tight junctions. Science, 344:304-307, 2014 Cited by PubMed Abstract: Tight junctions are cell-cell adhesion structures in epithelial cell sheets that surround organ compartments in multicellular organisms and regulate the permeation of ions through the intercellular space. Claudins are the major constituents of tight junctions and form strands that mediate cell adhesion and function as paracellular barriers. We report the structure of mammalian claudin-15 at a resolution of 2.4 angstroms. The structure reveals a characteristic β-sheet fold comprising two extracellular segments, which is anchored to a transmembrane four-helix bundle by a consensus motif. Our analyses suggest potential paracellular pathways with distinctive charges on the extracellular surface, providing insight into the molecular basis of ion homeostasis across tight junctions. PubMed: 24744376DOI: 10.1126/science.1248571 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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