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dc.contributor.authorTynan, FE
dc.contributor.authorBurrows, SR
dc.contributor.authorBuckle, AM
dc.contributor.authorClements, CS
dc.contributor.authorBorg, NA
dc.contributor.authorMiles, JJ
dc.contributor.authorBeddoe, T
dc.contributor.authorWhisstock, JC
dc.contributor.authorWilce, MC
dc.contributor.authorSilins, SL
dc.contributor.authorBurrows, JM
dc.contributor.authorKjer-Nielsen, L
dc.contributor.authorKostenko, L
dc.contributor.authorPurcell, AW
dc.contributor.authorMcCluskey, J
dc.contributor.authorRossjohn, J
dc.date.available2014-05-21T19:34:13Z
dc.date.available2005-08-23
dc.date.available2005-08-23
dc.date.available2005-08-23
dc.date.available2005-08-23
dc.date.available2005-08-23
dc.date.available2005-08-23
dc.date.available2005-08-23
dc.date.available2005-08-23
dc.date.available2005-08-23
dc.date.available2005-08-23
dc.date.available2005-08-23
dc.date.issued2005-11-01
dc.identifierpii: ni1257
dc.identifier.citationTynan, F. E., Burrows, S. R., Buckle, A. M., Clements, C. S., Borg, N. A., Miles, J. J., Beddoe, T., Whisstock, J. C., Wilce, M. C., Silins, S. L., Burrows, J. M., Kjer-Nielsen, L., Kostenko, L., Purcell, A. W., McCluskey, J. & Rossjohn, J. (2005). T cell receptor recognition of a 'super-bulged' major histocompatibility complex class I-bound peptide. NATURE IMMUNOLOGY, 6 (11), pp.1114-1122. https://doi.org/10.1038/ni1257.
dc.identifier.issn1529-2908
dc.identifier.urihttp://hdl.handle.net/11343/26474
dc.descriptionC1 - Journal Articles Refereed
dc.description.abstractUnusually long major histocompatibility complex (MHC) class I-restricted epitopes are important in immunity, but their 'bulged' conformation represents a potential obstacle to alphabeta T cell receptor (TCR)-MHC class I docking. To elucidate how such recognition is achieved while still preserving MHC restriction, we have determined here the structure of a TCR in complex with HLA-B(*)3508 presenting a peptide 13 amino acids in length. This complex was atypical of TCR-peptide-MHC class I interactions, being dominated at the interface by peptide-mediated interactions. The TCR assumed two distinct orientations, swiveling on top of the centrally bulged, rigid peptide such that only limited contacts were made with MHC class I. Although the TCR-peptide recognition resembled an antibody-antigen interaction, the TCR-MHC class I contacts defined a minimal 'generic footprint' of MHC-restriction. Thus our findings simultaneously demonstrate the considerable adaptability of the TCR and the 'shape' of MHC restriction.
dc.formatapplication/pdf
dc.languageEnglish
dc.publisherNATURE PUBLISHING GROUP
dc.subjectCellular Immunology; Immune System and Allergy
dc.titleT cell receptor recognition of a 'super-bulged' major histocompatibility complex class I-bound peptide
dc.typeJournal Article
dc.identifier.doi10.1038/ni1257
melbourne.peerreviewPeer Reviewed
melbourne.affiliationThe University of Melbourne
melbourne.affiliation.departmentMicrobiology And Immunology
melbourne.source.titleNATURE IMMUNOLOGY
melbourne.source.volume6
melbourne.source.issue11
melbourne.source.pages1114-1122
dc.research.coderfcd320202
dc.research.codeseo1998730102
melbourne.publicationid41327
melbourne.elementsid271459
melbourne.contributor.authorKjer-Nielsen, Lars
melbourne.contributor.authorKostenko, Lyudmila
melbourne.contributor.authorPURCELL, ANTHONY
melbourne.contributor.authorMcCluskey, James
dc.identifier.eissn1529-2916
pubs.acceptance.date2005-08-23
melbourne.accessrightsThis item is currently not available from this repository


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