Modulating the intrinsic disorder in the cytoplasmic domain alters the biological activity of the N-methyl-D-aspartatesensitive glutamate receptor

Abstract

Background: The NMDA-sensitive glutamate receptors contain disordered cytoplasmic domains that support isoformspecific signaling. Results: Proline residues dictate the conformational dynamics in disordered proteins, which were used to affect NMDA receptor activity. Conclusion: The intrinsically disordered cytoplasmic domain is involved in specific modes of NMDA receptor regulation. Significance: The underlying dynamics of protein disorder contribute to allosteric regulation. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.