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 belo
ngs to the immunoglobulin superfamily (IgSF), and its extracellular N-
terminal domain contains many conserved IgSF consensus residues seen i
n immunoglobulin variable region folds. The aim of the present study w
as 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 structu
re and binding characteristics. Molecular graphics techniques and mole
cular dynamics with secondary structure-based restraints were used in
the construction and refinement of the MOG model, Regions of high pred
iction confidence were identified, and possible glycosylation, dimeriz
ation, complement binding, and antibody-binding regions in MOG were ma
pped and analyzed.