突变型Vβ3 + T细胞受体的抗原识别特性与该受体的免疫球蛋白样结构一致。
Antigen recognition properties of mutant V beta 3+ T cell receptors are consistent with an immunoglobulin-like structure for the receptor.
作者信息
White J, Pullen A, Choi K, Marrack P, Kappler J W
机构信息
Howard Hughes Medical Institute, Department of Medicine, National Jewish Center for Immunology and Respiratory Medicine, Denver, Colorado.
出版信息
J Exp Med. 1993 Jan 1;177(1):119-25. doi: 10.1084/jem.177.1.119.
Abstract
We examined the effect of mutations in the V beta portion of a pigeon cytochrome c (cyto c)-specific V beta 3+/V alpha 11+ T cell receptor on its ability to recognize cyto c/IEk and various superantigens. The results were consistent with an immunoglobulin-like structure for the receptor V beta domain and with separate interaction sites on V beta for conventional antigen and superantigens. An amino acid predicted to lie in CDR1 was critical for cyto c/IEk but not superantigen recognition, while several amino acids predicted to lie in the hypervariable region 4 loop were critical for superantigen but not cyto c/IEk recognition.
摘要
我们研究了鸽细胞色素c（细胞色素c）特异性Vβ3+/Vα11+ T细胞受体的Vβ部分突变对其识别细胞色素c/IEk和各种超抗原能力的影响。结果与受体Vβ结构域的免疫球蛋白样结构一致，并且与Vβ上常规抗原和超抗原的独立相互作用位点一致。预测位于互补决定区1（CDR1）的一个氨基酸对细胞色素c/IEk识别至关重要，但对超抗原识别不重要，而预测位于高变区4环的几个氨基酸对超抗原识别至关重要，但对细胞色素c/IEk识别不重要。
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