T细胞受体
MHC限制
生物
主要组织相容性复合体
抗原
肽
T细胞
分子生物学
细胞生物学
生物化学
免疫系统
免疫学
作者
David N. Garboczi,Ursula Utz,Partho Ghosh,A Seth,Jongsun Kim,E A VanTienhoven,William E. Biddison,Don C. Wiley
出处
期刊:Journal of Immunology
[The American Association of Immunologists]
日期:1996-12-15
卷期号:157 (12): 5403-5410
被引量:148
标识
DOI:10.4049/jimmunol.157.12.5403
摘要
T lymphocytes use TCR-alphabeta to bind and to recognize complexes of antigenic peptides bound to MHC proteins located at the surface of APCs. We have assembled and crystallized this intercellular complex of TCR/peptide/MHC from soluble human TCR-alphabeta and soluble peptide/HLA-A2 complexes. The soluble TCR-alphabeta binds specifically to its in vivo ligand, the complex of HLA-A2, and a peptide from the Tax protein of human T lymphotropic virus type 1. The soluble TCR also binds in vitro to an altered peptide ligand, which appears to be a partial agonist in T cell assays as determined by its ability to elicit different cytolytic and lymphokine secretion responses. Heterodimerization and the antigenic specificity of the TCR do not require its interchain disulfide bond, transmembrane segments, or glycosylations. Crystals of the TCR/peptide/HLA-A2 complex diffract x-rays, providing the means to study in atomic detail the mechanism of Ag-specific cell-cell recognition between T cells and target cells.
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