6JOZ

Crystal structure of BRLF peptide from EBV in complex with HLA-A1101.

Summary for 6JOZ

• Entry DOI: 10.2210/pdb6joz/pdb
• Descriptor: HLA class I histocompatibility antigen, A-11 alpha chain, Beta-2-microglobulin, ALA-THR-ILE-GLY-THR-ALA-MET-TYR-LYS, ... (5 entities in total)
• Functional Keywords: immune system, human leukocyte antigen
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 3
• Total formula weight: 45204.01

Authors

Huan, X.,Xiao, Z.,Tadwal, V.S.,Ren, E.C. (deposition date: 2019-03-25, release date: 2020-01-29, Last modification date: 2024-10-23)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.35 Å)