Show simple item record

dc.contributor.authorClements, CS
dc.contributor.authorReid, HH
dc.contributor.authorBeddoe, T
dc.contributor.authorTynan, FE
dc.contributor.authorPerugini, MA
dc.contributor.authorJohns, TG
dc.contributor.authorBernard, CCA
dc.contributor.authorRossjohn, J
dc.date.available2014-05-21T19:39:01Z
dc.date.issued2003-09-16
dc.identifierpii: 1833158100
dc.identifier.citationClements, C. S., Reid, H. H., Beddoe, T., Tynan, F. E., Perugini, M. A., Johns, T. G., Bernard, C. C. A. & Rossjohn, J. (2003). The crystal structure of myelin oligodendrocyte glycoprotein, a key autoantigen in multiple sclerosis. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 100 (19), pp.11059-11064. https://doi.org/10.1073/pnas.1833158100.
dc.identifier.issn0027-8424
dc.identifier.urihttp://hdl.handle.net/11343/26584
dc.descriptionC1 - Journal Articles Refereed
dc.description.abstractMyelin 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.
dc.formatapplication/pdf
dc.languageEnglish
dc.publisherNATL ACAD SCIENCES
dc.subjectBiochemistry and Cell Biology not elsewhere classified ; Biological Sciences
dc.titleThe crystal structure of myelin oligodendrocyte glycoprotein, a key autoantigen in multiple sclerosis
dc.typeJournal Article
dc.identifier.doi10.1073/pnas.1833158100
melbourne.peerreviewPeer Reviewed
melbourne.affiliationThe University of Melbourne
melbourne.affiliation.departmentMedicine - Austin Health And Northern Health
melbourne.source.titlePROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
melbourne.source.volume100
melbourne.source.issue19
melbourne.source.pages11059-11064
dc.research.coderfcd270199
dc.research.codeseo1998780105
melbourne.publicationid19613
melbourne.elementsid258040
melbourne.openaccess.pmchttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC196926
melbourne.contributor.authorPerugini, Matthew
melbourne.contributor.authorJOHNS, TERRY
melbourne.contributor.authorCLEMENTS, CRAIG STEVEN
melbourne.contributor.authorBEDDOE, TRAVIS CLARKE
dc.identifier.eissn1091-6490
melbourne.accessrightsAccess this item via the Open Access location


Files in this item

FilesSizeFormatView

There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record