3FFC

Crystal Structure of CF34 TCR in complex with HLA-B8/FLR

3FFC の概要

• エントリーDOI: 10.2210/pdb3ffc/pdb
• 分子名称: HLA class I histocompatibility antigen, B-8 alpha chain, Beta-2-microglobulin, FLRGRAYGL peptide from an EBV protein, ... (9 entities in total)
• 機能のキーワード: tcr-peptide-mhc, glycoprotein, host-virus interaction, immune response, membrane, mhc i, transmembrane, disease mutation, glycation, immunoglobulin domain, pyrrolidone carboxylic acid, secreted, immune system
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 192377.27

構造登録者

Gras, S.,Burrows, S.R.,Kjer-Nielsen, L.,Clements, C.S.,Liu, Y.C.,Sullivan, L.C.,Brooks, A.G.,Purcell, A.W.,McCluskey, J.,Rossjohn, J. (登録日: 2008-12-03, 公開日: 2009-01-27, 最終更新日: 2024-10-30)

主引用文献

Gras, S.,Burrows, S.R.,Kjer-Nielsen, L.,Clements, C.S.,Liu, Y.C.,Sullivan, L.C.,Bell, M.J.,Brooks, A.G.,Purcell, A.W.,McCluskey, J.,Rossjohn, J.
The shaping of T cell receptor recognition by self-tolerance.
Immunity, 30:193-203, 2009

PubMed Abstract: During selection of the T cell repertoire, the immune system navigates the subtle distinction between self-restriction and self-tolerance, yet how this is achieved is unclear. Here we describe how self-tolerance toward a trans-HLA (human leukocyte antigen) allotype shapes T cell receptor (TCR) recognition of an Epstein-Barr virus (EBV) determinant (FLRGRAYGL). The recognition of HLA-B8-FLRGRAYGL by two archetypal TCRs was compared. One was a publicly selected TCR, LC13, that is alloreactive with HLA-B44; the other, CF34, lacks HLA-B44 reactivity because it arises when HLA-B44 is coinherited in trans with HLA-B8. Whereas the alloreactive LC13 TCR docked at the C terminus of HLA-B8-FLRGRAYGL, the CF34 TCR docked at the N terminus of HLA-B8-FLRGRAYGL, which coincided with a polymorphic region between HLA-B8 and HLA-B44. The markedly contrasting footprints of the LC13 and CF34 TCRs provided a portrait of how self-tolerance shapes the specificity of TCRs selected into the immune repertoire.

PubMed: 19167249
DOI: 10.1016/j.immuni.2008.11.011

実験手法

X-RAY DIFFRACTION (2.8 Å)