Effect of composition on the conformational dynamics of disordered cytosolic C-terminal of GluN2B protein involved in the multicomponent condensate formation

Abstract

N-methyl-D-aspartate receptors (NMDARs) are glutamate-gated ionotropic channels with high calcium permeability that play important roles in synaptic plasticity. The extracellular and transmembrane domains maintain the communication between pre- and post-synapse through ligand-induced changes in ion permeability, which have been extensively explored down to the atomic level. In contrast, structural and functional understanding of the intracellular C-terminal domain (CTD) remains still elusive. The long CTDs of GluN2 subunits recruit other proteins as part of the signaling pathways downstream of NMDARs, which have been linked to condensate formation through PSD-95 and SynGAP.