1zhl: Difference between revisions
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'''Crystal structure of HLA-B*3508 presenting 13-mer EBV antigen LPEPLPQGQLTAY''' | '''Crystal structure of HLA-B*3508 presenting 13-mer EBV antigen LPEPLPQGQLTAY''' | ||
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[[Category: Tynan, F E.]] | [[Category: Tynan, F E.]] | ||
[[Category: Zuylen, W J.van.]] | [[Category: Zuylen, W J.van.]] | ||
[[Category: | [[Category: Bulged epitope]] | ||
[[Category: | [[Category: T-cell receptor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:37:54 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 17:37, 3 May 2008
Crystal structure of HLA-B*3508 presenting 13-mer EBV antigen LPEPLPQGQLTAY
OverviewOverview
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.
About this StructureAbout this Structure
1ZHL is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
High resolution structures of highly bulged viral epitopes bound to major histocompatibility complex class I. Implications for T-cell receptor engagement and T-cell immunodominance., Tynan FE, Borg NA, Miles JJ, Beddoe T, El-Hassen D, Silins SL, van Zuylen WJ, Purcell AW, Kjer-Nielsen L, McCluskey J, Burrows SR, Rossjohn J, J Biol Chem. 2005 Jun 24;280(25):23900-9. Epub 2005 Apr 22. PMID:15849183 Page seeded by OCA on Sat May 3 17:37:54 2008