[5][6][7] It is speculated to serve as a necessary "adhesion molecule" to provide structural integrity to the myelin sheath and is known to develop late on the oligodendrocyte.

[12] The crystal structure of myelin oligodendrocyte glycoprotein was determined by x-ray diffraction at a resolution of 1.45 Angstroms, using protein from the Norway rat.

[15] Several features of the protein structure suggest MOG has a role as an "adhesin in the completion and/or compaction of the myelin sheath."

There is a "significant strip" of electronegative charge beginning near the N-terminus and running about half the length of the molecule.

Some of them are not-inflammatory, such as adrenoleukodystrophy, vanishing white matter disease, and Rubella induced mental retardation.

The proper way to identify it is by microarray, reacting patient serum with living cells, and detecting the binding IgG via a fluorescent-labeled secondary antibody.