2XFX

cattle MHC class I N01301 presenting an 11mer from Theileria parva

2XFX の概要

• エントリーDOI: 10.2210/pdb2xfx/pdb
• 関連するPDBエントリー: 1BMG
• 分子名称: MHC CLASS 1, BETA-2-MICROGLOBULIN, UNCHARACTERIZED PROTEIN, ... (4 entities in total)
• 機能のキーワード: immune system, major histocompatibility, east coast fever, theileriosis
• 由来する生物種: BOS TAURUS (CATTLE); 詳細
• 細胞内の位置: Secreted: P01888
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 45270.26

構造登録者

Macdonald, I.K.,Harkiolaki, M.,Hunt, L.,Morrison, W.I.,Connelley, T.,Graham, S.P.,Jones, E.Y.,Flower, D.R.,Ellis, S.A. (登録日: 2010-05-28, 公開日: 2010-10-27, 最終更新日: 2024-11-06)

主引用文献

Macdonald, I.K.,Harkiolaki, M.,Hunt, L.,Connelley, T.,Carroll, A.V.,Machugh, N.D.,Graham, S.P.,Jones, E.Y.,Morrison, W.I.,Flower, D.R.,Ellis, S.A.
Mhc Class I Bound to an Immunodominant Theileria Parva Epitope Demonstrates Unconventional Presentation to T Cell Receptors.
Plos Pathog., 6:01149-, 2010

PubMed Abstract: T cell receptor (TCR) recognition of peptide-MHC class I (pMHC) complexes is a crucial event in the adaptive immune response to pathogens. Peptide epitopes often display a strong dominance hierarchy, resulting in focusing of the response on a limited number of the most dominant epitopes. Such T cell responses may be additionally restricted by particular MHC alleles in preference to others. We have studied this poorly understood phenomenon using Theileria parva, a protozoan parasite that causes an often fatal lymphoproliferative disease in cattle. Despite its antigenic complexity, CD8+ T cell responses induced by infection with the parasite show profound immunodominance, as exemplified by the Tp1(214-224) epitope presented by the common and functionally important MHC class I allele N*01301. We present a high-resolution crystal structure of this pMHC complex, demonstrating that the peptide is presented in a distinctive raised conformation. Functional studies using CD8+ T cell clones show that this impacts significantly on TCR recognition. The unconventional structure is generated by a hydrophobic ridge within the MHC peptide binding groove, found in a set of cattle MHC alleles. Extremely rare in all other species, this feature is seen in a small group of mouse MHC class I molecules. The data generated in this analysis contribute to our understanding of the structural basis for T cell-dependent immune responses, providing insight into what determines a highly immunogenic p-MHC complex, and hence can be of value in prediction of antigenic epitopes and vaccine design.

PubMed: 20976198
DOI: 10.1371/JOURNAL.PPAT.1001149

実験手法

X-RAY DIFFRACTION (1.9 Å)