A molecular model of myelin oligodendrocyte glycoprotein

J Neurochem. 1998 Oct;71(4):1742-9. doi: 10.1046/j.1471-4159.1998.71041742.x.


Myelin oligodendrocyte glycoprotein (MOG) is a protein on the surface of myelin sheaths. It is a putative target of the autoimmune attack in the inflammatory and demyelinating CNS disease multiple sclerosis and its animal model, experimental autoimmune encephalomyelitis. MOG belongs to the immunoglobulin superfamily (IgSF), and its extracellular N-terminal domain contains many conserved IgSF consensus residues seen in immunoglobulin variable region folds. The aim of the present study was to create a molecular model of the extracellular N-terminal domain of mouse MOG. No crystal structure is yet available of MOG, and thus a molecular model would be useful in providing insight into its structure and binding characteristics. Molecular graphics techniques and molecular dynamics with secondary structure-based restraints were used in the construction and refinement of the MOG model. Regions of high prediction confidence were identified, and possible glycosylation, dimerization, complement binding, and antibody-binding regions in MOG were mapped and analyzed.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Complement System Proteins / metabolism
  • Computer Simulation
  • Dimerization
  • Glycosylation
  • Humans
  • Immunoglobulins / chemistry
  • Mice
  • Models, Molecular*
  • Molecular Sequence Data
  • Myelin Proteins
  • Myelin-Associated Glycoprotein / chemistry*
  • Myelin-Oligodendrocyte Glycoprotein
  • Protein Binding
  • Protein Folding
  • Sequence Homology, Amino Acid


  • Immunoglobulins
  • MOG protein, human
  • Mog protein, mouse
  • Myelin Proteins
  • Myelin-Associated Glycoprotein
  • Myelin-Oligodendrocyte Glycoprotein
  • Complement System Proteins