Conformational and Dynamic Properties of Extracellular Domains of Cell Adhesion Molecules

Due to their specific binding properties, cell adhesion molecules (CAMs), such as integrin, cadherin and the immunoglobulin superfamily CAMs are of primary importance in cell-cell and cell-substrate interactions, signaling pathways and other crucial biological processes. We investigate the molecular structures and conformational dynamics of the extracellular domains of the Aplysia CAM (apCAM), by constructing and studying their atomically detailed structural model based on homology with human neural CAM (NCAM). The stability and dynamic properties of the apCAM domains, individually and as a connected in the molecule, are probed and analyzed using all-atom explicit-solvent molecular dynamics simulations. The refined structural model reveals a specific pattern of amino acid interactions that controls the stability of their beta-sheet reach structures, and which could affect their specific response to environmental changes.