1ZHK

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

Summary for 1ZHK

• Entry DOI: 10.2210/pdb1zhk/pdb
• Related: 1ZHL
• Descriptor: HLA class I histocompatibility antigen, B-35 alpha chain, Beta-2-microglobulin, EBV-peptide LPEPLPQGQLTAY, ... (4 entities in total)
• Functional Keywords: t-cell receptor, bulged epitopes, immune system
• Biological source: Homo sapiens (human); More
• Cellular location: Membrane; Single-pass type I membrane protein: P30685; Secreted: P61769
• Total number of polymer chains: 3
• Total formula weight: 45115.02

Authors

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. (deposition date: 2005-04-26, release date: 2005-05-17, Last modification date: 2024-10-16)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.6 Å)