Reactions of anti-immunoglobulin sera with synthetic T cell receptor peptides: implications for the three-dimensional structure and function of the TCR beta chain.
Reactions of anti-immunoglobulin sera with synthetic T cell receptor peptides: implications for the three-dimensional structure and function of the TCR beta chain.
复制标题
抗免疫球蛋白血清与合成 T 细胞受体肽的反应：对 TCR β 链三维结构和功能的影响。
DOI：
10.1093/intimm/5.5.491
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发表时间：
1993
影响因子：
4.4
通讯作者：
Marchalonis,JJ
中科院分区：
文献类型：
--
作者：
Kaymaz,H;Dedeoglu,F;Schluter,SF;Edmundson,AB;Marchalonis,JJ
人类TCR β链的氨基酸序列在其可变(V)和恒定(C)结构域以及连接段(J)中与lg λ轻链具有相当的同源性。我们通过合成一组嵌套的、重叠的16聚肽来评估TCR β链和lg轻链之间的交叉反应性，这些肽复制了TCR β链连续VDJC序列的序列，并测定了兔抗血清与人或小鼠抗血清与这些肽的反应能力。我们观察到的反应性与λ和xlight链的同源性一致。在ELISA结合和竞争性抑制中，反应性最强的是与轻链“开关肽”对应的肽。该序列由J段的C端区（Fr4）和C区的n端部编码。与抗轻链血清反应的其他区域分别对应于V区的CDR1和Fr3片段，以及预测将环出紧密球形结构的恒定区片段。肽免疫化学结果，再加上TCR β和表征的λ轻链Mcg之间序列对应的特定区域的鉴定，使我们能够建立β链的三维模型，与它在抗原识别和对超抗原的反应中所起的作用一致。
The derived amino acid sequence of the human TCR β chain shows considerable homology to lg λ light chains in its variable (V) and constant (C) domains, and in its joining segment (J). We assessed the cross-reactivity between TCR β chains and lg light chains by synthesizing a set of nested, overlapping 16-mer peptides that duplicated the sequence that corresponds to the continuous VDJC sequence of TCR β chain and determining the capacity of rabbit antisera to human or murine lgs to react with these peptides. The reactivities we observed were consistent with homologies to λ andxlight chains. The strongest reactivity in ELISA binding and competitive inhibition was with a peptide that corresponds to the ‘swtch peptide’ of light chains. The sequence is encoded by the C-terminal region of the J segment (Fr4) and the N-termlnus of the C region. Other regions reactive with anti-light chain sera corresponded respectively to CDR1 and Fr3 segments of the V region, and a segment of the constant region predicted to loop out of the tight globular structure. The peptide immunochemical results, coupled with the identification of specific regions of sequence correspondence between TCR β and the characterized λ light chain Mcg, allowed us to develop a three-dimensional model of the β chain consistent with its role in antigen recognition and response to superantigens.