1Q1P

E-Cadherin activation

Summary for 1Q1P

• Entry DOI: 10.2210/pdb1q1p/pdb
• Related: 1FF5
• Descriptor: Epithelial-cadherin, CALCIUM ION (3 entities in total)
• Functional Keywords: cell adhesion
• Biological source: Mus musculus (mouse)
• Cellular location: Cell junction: P09803
• Total number of polymer chains: 1
• Total formula weight: 23266.01

Authors

Haussinger, D.,Stetefeld, J. (deposition date: 2003-07-22, release date: 2004-04-20, Last modification date: 2023-08-16)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.2 Å)