1q1p

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Image:1q1p.gif

1q1p, resolution 3.20Å

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E-Cadherin activation

Overview

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.

About this Structure

1Q1P is a Single protein structure of sequence from Mus musculus with as ligand. Full crystallographic information is available from OCA.

Reference

Proteolytic E-cadherin activation followed by solution NMR and X-ray crystallography., Haussinger D, Ahrens T, Aberle T, Engel J, Stetefeld J, Grzesiek S, EMBO J. 2004 Apr 21;23(8):1699-708. Epub 2004 Apr 8. PMID:15071499

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