1ZHK

Crystal structure of HLA-B*3501 presenting 13-mer EBV antigen LPEPLPQGQLTAY

1ZHK の概要

• エントリーDOI: 10.2210/pdb1zhk/pdb
• 関連するPDBエントリー: 1ZHL
• 分子名称: HLA class I histocompatibility antigen, B-35 alpha chain, Beta-2-microglobulin, EBV-peptide LPEPLPQGQLTAY, ... (4 entities in total)
• 機能のキーワード: t-cell receptor, bulged epitopes, immune system
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P30685; Secreted: P61769
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 45115.02

構造登録者

Tynan, F.E.,Borg, N.A.,Miles, J.J.,Beddoe, T.,El-Hassen, D.,Silins, S.L.,van Zuylen, W.J.,Purcell, A.W.,Kjer-Nielsen, L.,McCluskey, J.,Burrows, S.R.,Rossjohn, J. (登録日: 2005-04-26, 公開日: 2005-05-17, 最終更新日: 2024-10-16)

主引用文献

Tynan, F.E.,Borg, N.A.,Miles, J.J.,Beddoe, T.,El-Hassen, D.,Silins, S.L.,van Zuylen, W.J.,Purcell, A.W.,Kjer-Nielsen, L.,McCluskey, J.,Burrows, S.R.,Rossjohn, J.
The high resolution structures of highly bulged viral epitopes bound to the major histocompatability class I: Implications for T-cell receptor engagement and T-cell immunodominance
J.Biol.Chem., 280:23900-23909, 2005

PubMed Abstract: Although HLA class I alleles can bind epitopes up to 14 amino acids in length, little is known about the immunogenicity or the responding T-cell repertoire against such determinants. Here, we describe an HLA-B*3508-restricted cytotoxic T lymphocyte response to a 13-mer viral epitope (LPEPLPQGQLTAY). The rigid, centrally bulged epitope generated a biased T-cell response. Only the N-terminal face of the peptide bulge was critical for recognition by the dominant clonotype SB27. The SB27 public T-cell receptor (TcR) associated slowly onto the complex between the bulged peptide and the major histocompatibility complex, suggesting significant remodeling upon engagement. The broad antigen-binding cleft of HLA-B*3508 represents a critical feature for engagement of the public TcR, as the narrower binding cleft of HLA-B*3501(LPEPLPQGQLTAY), which differs from HLA-B*3508 by a single amino acid polymorphism (Arg156 --> Leu), interacted poorly with the dominant TcR. Biased TcR usage in this cytotoxic T lymphocyte response appears to reflect a dominant role of the prominent peptide x major histocompatibility complex class I surface.

PubMed: 15849183
DOI: 10.1074/jbc.M503060200

実験手法

X-RAY DIFFRACTION (1.6 Å)