Dynamics and stability of E-cadherin dimers.

ABSTRACT: The extracellular domains of cadherins are known to play a major role in cell adhesion, although the structures involved in this process remain unclear. We have used molecular dynamics to characterize the conformational and thermodynamic properties of two of the dimer interfaces identified in E-cadherin crystals and involving the two outermost exodomains (EC1 and EC2): a dimer involving exchange of the N-terminal strand (referred to as the "swapped" dimer) and a "staggered" dimer involving an EC1-EC2 interface. The results show that the staggered dimer involves a much smaller interface area and is notably less stable than the swapped dimer. It is also found that, despite its stability, the swapped dimer undergoes a conformational transition leading to a structure closer to that experimenta

SUBMITTER: Cailliez F 

PROVIDER: S-EPMC1635664 | biostudies-literature | 2006 Dec

REPOSITORIES: biostudies-literature