Homomeric Interactions Between IG Domains of the MPZ (P0) Myelin Adhesion Protein Provide Structural Context for Multiple Disease Mechanisms

Myelin protein zero (MPZ) is a structural transmembrane protein and a major component of peripheral myelin that holds tightly compacted adjacent membrane layers together. The extracellular immunoglobulin-like domain of MPZ (IgMPZ) is thought to adhere apposing membranes together through homomeric interactions; however, the multiple weak interfaces that occur within the IgMPZ crystal structure fail to provide a definitive model for this assembly. Here, equilibrium distributions for IgMPZ oligomeric populations were obtained in solution using NMR and SAXS.