Interactions between downstream regulatory element antagonist modulator (DREAM) and presenilin 1 (PS1) are related to numerous neuronal processes. We demonstrate that association of PS1 carboxyl peptide (residues 445-467, HL9) with DREAM is calcium dependent and stabilized by a cluster of three aromatic residues: F462 and F465 from PS1 and F252 from DREAM. Additional stabilization is provided by residues in a loop connecting α helices 7 and 8 in DREAM and residues of PS1, namely cation-π interactions between R200 in DREAM and F465 in PS1 and the salt bridges formed by R207 in DREAM and D450 and D458 in PS1.
Keywords: Alzheimer's disease; DREAM; calsenilin; fluorescence anisotropy; potassium channel interacting protein; presenilin-binding interfaces.
© 2016 Federation of European Biochemical Societies.