1py9
From Proteopedia
|
The crystal structure of an autoantigen in multiple sclerosis
Overview
Myelin oligodendrocyte glycoprotein (MOG) is a key CNS-specific, autoantigen for primary demyelination in multiple sclerosis. Although the, disease-inducing role of MOG has been established, its precise function in, the CNS remains obscure. To gain new insights into the physiological and, immunopathological role of MOG, we determined the 1.8-A crystal structure, of the MOG extracellular domain (MOGED). MOGED adopts a classical Ig (Ig, variable domain) fold that was observed to form an antiparallel, head-to-tail dimer. A dimeric form of native MOG was observed, and MOGED, was also shown to dimerize in solution, consistent with the view of MOG, acting as a homophilic adhesion receptor. The MOG35-55 peptide, a major, encephalitogenic determinant recognized by both T cells and demyelinating, autoantibodies, is partly occluded within the dimer interface. The, structure of this key autoantigen suggests a relationship between the, dimeric form of MOG within the myelin sheath and a breakdown of, immunological tolerance to MOG that is observed in multiple sclerosis.
About this Structure
1PY9 is a Single protein structure of sequence from Mus musculus with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
The crystal structure of myelin oligodendrocyte glycoprotein, a key autoantigen in multiple sclerosis., Clements CS, Reid HH, Beddoe T, Tynan FE, Perugini MA, Johns TG, Bernard CC, Rossjohn J, Proc Natl Acad Sci U S A. 2003 Sep 16;100(19):11059-64. Epub 2003 Sep 5. PMID:12960396
Page seeded by OCA on Wed Nov 21 00:13:36 2007
