Abstract:
: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.
journal_name
J Neurochemjournal_title
Journal of neurochemistryauthors
Hjelmström P,Penzotti JE,Henne RM,Lybrand TPdoi
10.1046/j.1471-4159.1998.71041742.xsubject
Has Abstractpub_date
1998-10-01 00:00:00pages
1742-9issue
4eissn
0022-3042issn
1471-4159journal_volume
71pub_type
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