Anti-MOG associated inflammatory demyelinating diseases Some of them are not-inflammatory, such as adrenoleukodystrophy, vanishing white matter disease, and Rubella induced mental retardation. Interest in MOG has centered on its role in demyelinating diseases. Role in disease Non-inflammatory demyelinating diseases Also, MOG was shown to dimerize in solution, and the shape complementarity index is high at the dimer interface, suggesting a 'biologically relevant MOG dimer.' Synthesis ĭevelopmentally, MOG is formed 'very late on oligodendrocytes and the myelin sheath'. 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. The beta strands are within two antiparallel beta sheets that form an immunoglobulin-like beta-sandwich fold.

The dssp secondary structure of the protein is 6% helical and 43% beta sheet: there are three short helical segments and ten beta strands. This protein is 139 residues long, and is a member of the immunoglobulin superfamily. 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. The introns 'contain numerous reptitive DNA ' sequences, among which are '14 Alu sequences within 3 introns', and have a range varying from 242 to 6484 bp.Īlternatively spliced human mRNA of the MOG gene form at least nine isoforms. The MOG 'primary nuclear transcript … is 15,561 nucleotides in length' and, for humans, it has eight exons which are 'separated by seven introns'. and therefore is easily accessible to autoantibodies too. 'A single Ig-domain is exposed to the extracellular space' and consequently allows autoantibodies easy access. 'MOG is a quantitatively minor type I transmembrane protein, and is found exclusively in the CNS. It is a transmembrane protein expressed on the surface of oligodendrocyte cell and on the outermost surface of myelin sheaths. The gene for MOG, found on chromosome 6 p21.3-p22, was first sequenced in 1995. This suggests 'an important biological role for this protein'. MOG's cDNA coding region in humans have been shown to be 'highly homologous' to rats, mice, and bovine, and hence highly conserved. More specifically, MOG is speculated to be 'necessary' as an 'adhesion molecule' on the myelin sheath of the CNS to provide the structural integrity of the myelin sheath. While the primary molecular function of MOG is not yet known, its likely role with the myelin sheath is either in sheath 'completion and/or maintenance'. 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. In humans this protein is encoded by the MOG gene. Myelin oligodendrocyte glycoprotein ( MOG) is a glycoprotein believed to be important in the myelination of nerves in the central nervous system (CNS).

Mog neuro