1PY9

The crystal structure of an autoantigen in multiple sclerosis

1PY9 の概要

• エントリーDOI: 10.2210/pdb1py9/pdb
• 分子名称: Myelin-oligodendrocyte glycoprotein, SULFATE ION (3 entities in total)
• 機能のキーワード: myelin sheath, multiple sclerosis, receptor, immunoglobulin, anti-parallel dimer, immune system
• 由来する生物種: Mus musculus (house mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13469.95

構造登録者

Clements, C.S.,Reid, H.H.,Beddoe, T.,Tynan, F.E.,Perugini, M.A.,Johns, T.G.,Bernard, C.C.,Rossjohn, J. (登録日: 2003-07-08, 公開日: 2003-09-30, 最終更新日: 2024-10-16)

主引用文献

Clements, C.S.,Reid, H.H.,Beddoe, T.,Tynan, F.E.,Perugini, M.A.,Johns, T.G.,Bernard, C.C.,Rossjohn, J.
The crystal structure of myelin oligodendrocyte glycoprotein, a key autoantigen in multiple sclerosis
Proc.Natl.Acad.Sci.USA, 100:11059-11064, 2003

PubMed Abstract: 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.

PubMed: 12960396
DOI: 10.1073/pnas.1833158100

実験手法

X-RAY DIFFRACTION (1.8 Å)