4P79

Crystal structure of mouse claudin-15

4P79 の概要

• エントリーDOI: 10.2210/pdb4p79/pdb
• 分子名称: Claudin-15, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate (3 entities in total)
• 機能のキーワード: cell adhesion, tight junction, membrane protein, paracellular channel
• 由来する生物種: Mus musculus (Mouse)
• 細胞内の位置: Cell junction, tight junction: Q9Z0S5
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22157.74

構造登録者

Suzuki, H.,Nishizawa, T.,Tani, K.,Yamazaki, Y.,Tamura, A.,Ishitani, R.,Dohmae, N.,Tsukita, S.,Nureki, O.,Fujiyoshi, Y. (登録日: 2014-03-26, 公開日: 2014-04-30, 最終更新日: 2024-11-20)

主引用文献

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

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: 24744376
DOI: 10.1126/science.1248571

実験手法

X-RAY DIFFRACTION (2.4 Å)