文章基本信息

标题：Alloreactivity studied with mutants of HLA-A2
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作者：J Santos-Aguado ; M A Crimmins ; S J Mentzer 等
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：1989
卷号：86
期号：22
页码：8936-8940
DOI：10.1073/pnas.86.22.8936
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Based on the crystal structure of HLA-A2.1 and the recognition of a panel of mutant HLA-A2.1 molecules by a large number of alloreactive cytotoxic T lymphocyte clones, a model to explain alloreactivity is described. In this model recognition of an allogeneic major histocompatibility complex molecule by a self-restricted T-cell receptor occurs as the result of accommodation by the receptor of a few amino acid differences in the major histocompatibility complex molecule--i.e., cross-recognition. Alloreactivity is the result of the presence in the foreign antigen binding site of the allogeneic major histocompatibility complex molecule of unusual self-peptides, reactivity to which could not have been eliminated by negative thymic selection.