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Biophys. J. BioFAST: First Published September 23, 2005. doi:10.1529/biophysj.105.067322
© 2005 by the Biophysical Society.

A more recent version of this article appeared on December 1, 2005.
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BIOPHYSICAL THEORY AND MODELING

Cadherin mechanics and complexation: the importance of calcium binding

Fabien Cailliez 1 and Richard Lavery 1*

1 Institut de Biologie Physico-Chimique

* To whom correspondence should be addressed. E-mail: rlavery{at}ibpc.fr.

Submitted on May 25, 2005
Revised on July 5, 2005
Accepted on 13 September 2005


  Abstract
E-cadherins belong to a family of membrane bound, cellular adhesion proteins. Their adhesive properties mainly involve the two N-terminal extracellular domains (EC1 and EC2). The junctions between these domains are characterized by calcium ion binding sites and calcium ions are essential for the correct functioning of E-cadherins. Calcium is believed to rigidify the extra-cellular portion of the protein, which, when complexed, adopts a rod-like conformation. Here, we use molecular dynamics simulations to investigate the dynamics of the EC1-2 portion of E-cadherin in the presence and in the absence of calcium ions. These simulations confirm that apo-cadherin shows much higher conformational flexibility on a nanosecond timescale than the calcium bound form. It is also shown that although the apo-cadherin fragment can spontaneously complex potassium, these monovalent ions are incapable of rigidifying the inter-domain junctions. In contrast, removal of the most solvent-exposed calcium ion at the EC1-2 junction does not significantly perturb the dynamical behavior of the fragment. We have also extended this study to the cis-dimer formed from two EC1-2 fragments, potentially involved in cellular adhesion. Here again, it is shown that the presence of calcium is an important factor in both rigidifying and stabilizing the complex.

Key Words: Cellular adhesion, E-cadherin, Ion binding, Molecular dynamics, Protein mechanics




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Copyright © 2005 by the Biophysical Society.