Calmodulin interactions with model lipid membranes: the interplay of Ca2+and lipid composition

Abstract

Interactions of ionic proteins and lipids are believed to be crucial for the structure and function of membrane receptors and ion-channels. Calmodulin (CaM) is a highly conserved, multifunctional calcium-modulated protein, expressed in all eukaryotic cells. It binds to a wide variety of target proteins, influencing their function. Moreover, CaM binds up to four calcium ions through four EF-hand motifs, consisting of helix-loop-helix domains. This is known to lead to a conformational change that allows the binding with other target proteins, essential in many biological processes and driven by hydrophobic interactions.