Structural Properties of the Myelin‐Associated Glycoprotein Ectodomain

Abstract

Myelin-associated glycoprotein (MAG) has been proposed to mediate adhesive interactions during myelin development. We have used the baculovirus expression system to produce a truncated form of this molecule [soluble extracellular domain of MAG (sMAG)] consisting of the complete extracellular ectodomain. Spectroscopic studies indicate a high beta-sheet content, consistent with the prediction of Ig-like structure. Hydrodynamic studies indicate an asymmetric monomer, with a Stokes radius of 4.1-4.6 nm, a sedimentation coefficient of 3.6S, and a frictional ratio of approximately 1.6. We postulate that the outer two Ig-like domains form a unit that folds back over the rest of the molecule. Fluorescence quenching studies indicate that sMAG interacts with divalent cations and may have a functional lectin domain.