1Q1P

E-Cadherin activation

1Q1P の概要

• エントリーDOI: 10.2210/pdb1q1p/pdb
• 関連するPDBエントリー: 1FF5
• 分子名称: Epithelial-cadherin, CALCIUM ION (3 entities in total)
• 機能のキーワード: cell adhesion
• 由来する生物種: Mus musculus (mouse)
• 細胞内の位置: Cell junction: P09803
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23266.01

構造登録者

Haussinger, D.,Stetefeld, J. (登録日: 2003-07-22, 公開日: 2004-04-20, 最終更新日: 2023-08-16)

主引用文献

Haussinger, D.,Ahrens, T.,Aberle, T.,Engel, J.,Stetefeld, J.,Grzesiek, S.
Proteolytic E-cadherin activation followed by solution NMR and X-ray crystallography.
Embo J., 23:1699-1708, 2004

PubMed Abstract: Cellular adhesion by classical cadherins depends critically on the exact proteolytic removal of their N-terminal prosequences. In this combined solution NMR and X-ray crystallographic study, the consequences of propeptide cleavage of an epithelial cadherin construct (domains 1 and 2) were followed at atomic level. At low protein concentration, the N-terminal processing induces docking of the tryptophan-2 side-chain into a binding pocket on the same molecule. At high concentration, cleavage induces dimerization (KD=0.72 mM, k(off)=0.7 s(-1)) and concomitant intermolecular exchange of the betaA-strands and the tryptophan-2 side-chains. Thus, the cleavage represents the switch from a nonadhesive to the functional form of cadherin.

PubMed: 15071499
DOI: 10.1038/sj.emboj.7600192

実験手法

X-RAY DIFFRACTION (3.2 Å)