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dc.contributor.authorMcMahon, Roisin M
dc.contributor.authorFriis, Lone
dc.contributor.authorSiebold, Christian
dc.contributor.authorFriese, Manuel A
dc.contributor.authorFugger, Lars
dc.contributor.authorJones, E Yvonne
dc.date.accessioned2019-03-22T02:40:24Z
dc.date.available2019-03-22T02:40:24Z
dc.date.issued2011
dc.identifier.issn0907-4449
dc.identifier.doi10.1107/S0907444911007888
dc.identifier.urihttp://hdl.handle.net/10072/172517
dc.description.abstractThe structure of the human major histocompatability (MHC) class I molecule HLA-A*0301 (HLA-A3) in complex with a nonameric peptide (KLIETYFSK) has been determined by X-­ray crystallography to 2.7 Å resolution. HLA-A3 is a predisposing allele for multiple sclerosis (MS), an auto­immune disease of the central nervous system. The KLIETYFSK peptide is a naturally processed epitope of proteolipid protein, a myelin protein and candidate target for immune-mediated myelin destruction in MS. Comparison of the structure of HLA-A3 with that of HLA-A2, an MHC class I molecule which is protective against MS, indicates that both MHC class I molecules present very similar faces for T-cell receptor recognition whilst differing in the specificity of their peptide-binding grooves. These characteristics may underlie the opposing (predisposing versus protective) associations that they exhibit both in humans and in mouse models of MS-­like disease. Furthermore, subtle alterations within the peptide-binding groove of HLA-A3 and other A3-like MHC class I molecules, members of the so-called A3 superfamily, may be sufficient to alter their presentation of autoantigen peptides such as KLIETYFSK. This in turn may modulate their contribution to the associated risk of autoimmune disease.
dc.description.peerreviewedYes
dc.languageEnglish
dc.publisherWiley-Blackwell Publishing
dc.relation.ispartofpagefrom447
dc.relation.ispartofpageto454
dc.relation.ispartofissue5
dc.relation.ispartofjournalActa Crystallographica Section D: Biological Crystallography
dc.relation.ispartofvolume67
dc.subject.fieldofresearchMedicinal and Biomolecular Chemistry not elsewhere classified
dc.subject.fieldofresearchChemical Sciences
dc.subject.fieldofresearchBiological Sciences
dc.subject.fieldofresearchPhysical Sciences
dc.subject.fieldofresearchcode030499
dc.subject.fieldofresearchcode03
dc.subject.fieldofresearchcode06
dc.subject.fieldofresearchcode02
dc.titleStructure of HLA-A*0301 in complex with a peptide of proteolipid protein: Insights into the role of HLA-A alleles in susceptibility to multiple sclerosis
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.rights.copyright© 2011 International Union of Crystallography. This is the Authorised Electronic Reprint version of the following article: Structure of HLA-A*0301 in complex with a peptide of proteolipid protein: Insights into the role of HLA-A alleles in susceptibility to multiple sclerosis, Acta Crystallographica Section D, D67, 447-454, which has been published in final form at 10.1107/S0907444911007888
gro.hasfulltextFull Text
gro.griffith.authorMcMahon, Roisin


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