2nw3
|
Crystal structure of HLA-B*3508 presenting EBV peptide EPLPQGQLTAY at 1.7A
OverviewOverview
Plasticity of the T cell receptor (TCR) is a hallmark of major, histocompatibility complex (MHC)-restricted T cell recognition. However, it is unclear whether interactions of TCR and peptide-MHC class I (pMHCI), always conform to this paradigm. Here we describe the structure of a TCR, ELS4, in its non-ligand-bound form and in complex with a prominent, 'bulged' Epstein-Barr virus peptide bound to HLA-B(*)3501. This complex, was atypical of previously characterized TCR-pMHCI interactions in that a, rigid face of the TCR crumpled the bulged antigenic determinant. This, peptide 'bulldozing' created a more featureless pMHCI determinant, allowing the TCR to maximize MHC class I contacts essential for MHC class, I restriction of TCR recognition. Our findings represent a mechanism of, antigen recognition whereby the plasticity of the T cell response is, dictated mainly by adjustments in the MHC-bound peptide.
DiseaseDisease
Known diseases associated with this structure: Abacavir hypersensitivity, susceptibility to OMIM:[142830], Hypoproteinemia, hypercatabolic OMIM:[109700], Spondyloarthropathy, susceptibility to, 1 OMIM:[142830], Stevens-Johnson syndrome, carbamazepine-induced, susceptibility to OMIM:[142830]
About this StructureAbout this Structure
2NW3 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule., Tynan FE, Reid HH, Kjer-Nielsen L, Miles JJ, Wilce MC, Kostenko L, Borg NA, Williamson NA, Beddoe T, Purcell AW, Burrows SR, McCluskey J, Rossjohn J, Nat Immunol. 2007 Mar;8(3):268-76. Epub 2007 Jan 28. PMID:17259989
Page seeded by OCA on Mon Nov 12 23:03:12 2007