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  • 标题:Structure of UL18, a peptide-binding viral MHC mimic, bound to a host inhibitory receptor
  • 本地全文:下载
  • 作者:Zhiru Yang ; Pamela J. Bjorkman
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:2008
  • 卷号:105
  • 期号:29
  • 页码:10095-10100
  • DOI:10.1073/pnas.0804551105
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:UL18 is a human cytomegalovirus class I MHC (MHCI) homolog that binds the host inhibitory receptor LIR-1 and the only known viral MHC homolog that presents peptides. The 2.2-A structure of a LIR-1/UL18/peptide complex reveals increased contacts and optimal surface complementarity in the LIR-1/UL18 interface compared with LIR/MHCI interfaces, resulting in a >1,000-fold higher affinity. Despite sharing only {approx}25% sequence identity, UL18's structure and peptide binding are surprisingly similar to host MHCI. The crystal structure suggests that most of the UL18 surface, except where LIR-1 and the host-derived light chain bind, is covered by carbohydrates attached to 13 potential N-glycosylation sites, thereby preventing access to bound peptide and association with most MHCI-binding proteins. The LIR-1/UL18 structure demonstrates how a viral protein evolves from its host ancestor to impede unwanted interactions while preserving and improving its receptor-binding site.
  • 关键词:cytomegalovirus ; immune evasion ; LIR-1 ; x-ray crystallography
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