1PY9
The crystal structure of an autoantigen in multiple sclerosis
Summary for 1PY9
| Entry DOI | 10.2210/pdb1py9/pdb |
| Descriptor | Myelin-oligodendrocyte glycoprotein, SULFATE ION (3 entities in total) |
| Functional Keywords | myelin sheath, multiple sclerosis, receptor, immunoglobulin, anti-parallel dimer, immune system |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 13469.95 |
| Authors | Clements, C.S.,Reid, H.H.,Beddoe, T.,Tynan, F.E.,Perugini, M.A.,Johns, T.G.,Bernard, C.C.,Rossjohn, J. (deposition date: 2003-07-08, release date: 2003-09-30, Last modification date: 2024-10-16) |
| Primary citation | 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 Cited by 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: 12960396DOI: 10.1073/pnas.1833158100 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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