6JP3

Crystal structure of peptide in complex with HLA-A1101.

6JP3 の概要

• エントリーDOI: 10.2210/pdb6jp3/pdb
• 分子名称: HLA class I histocompatibility antigen, A-11 alpha chain, Beta-2-microglobulin, ALA-THR-ILE-GLY-THR, ... (6 entities in total)
• 機能のキーワード: immune system, human leukocyte antigen
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 44945.74

構造登録者

Huan, X.,Xiao, Z.,Ren, E.C. (登録日: 2019-03-25, 公開日: 2020-01-29, 最終更新日: 2024-10-16)

主引用文献

Huan, X.,Zhuo, Z.,Xiao, Z.,Ren, E.C.
Crystal structure of suboptimal viral fragments of Epstein Barr Virus Rta peptide-HLA complex that stimulate CD8 T cell response.
Sci Rep, 9:16660-16660, 2019

PubMed Abstract: Peptides presented by Human leukocyte antigen (HLA) class-I molecules are generally 8-10 amino acids in length. However, the predominant pool of peptide fragments generated by proteasomes is less than 8 amino acids in length. Using the Epstein - Barr virus (EBV) Rta-epitope (ATIGTAMYK, residues 134-142) restricted by HLA-A*11:01 which generates a strong immunodominant response, we investigated the minimum length of a viral peptide that can constitute a viral epitope recognition by CD8 T cells. The results showed that Peripheral blood mononuclear cells (PBMCs) from healthy donors can be stimulated by a viral peptide fragment as short as 4-mer (AMYK), together with a 5-mer (ATIGT) to recapitulate the full length EBV Rta epitope. This was confirmed by generating crystals of the tetra-complex (2 peptides, HLA and β2-microglobulin). The solved crystal structure of HLA-A*11:01 in complex with these two short peptides revealed that they can bind in the same orientation similar to parental peptide (9-mer) and the free ends of two short peptides acquires a bulged conformation that is directed towards the T cell receptor. Our data shows that suboptimal length of 4-mer and 5-mer peptides can complement each other to form a stable peptide-MHC (pMHC) complex.

PubMed: 31723204
DOI: 10.1038/s41598-019-53201-6

実験手法

X-RAY DIFFRACTION (1.66 Å)