Primary structure of human T-cell receptor alpha-chain.
Primary structure of human T-cell receptor alpha-chain.
复制标题
人类 T 细胞受体 α 链的一级结构。
作者：
Sim,GK;Yagüe,J;Nelson,J;Marrack,P;Palmer,E;Augustin,A;Kappler,J
为了了解主要组织相容性复合体（MHC）限制性抗原识别的分子基础，在过去的10年里，人们对t细胞受体进行了深入的研究。利用抗受体单克隆抗体从人和鼠t细胞克隆10 - 15中分离和表征该受体，表明该蛋白由两个二硫连接的糖肽α和β组成，不同于已知的免疫球蛋白轻链和重链。然而，与免疫球蛋白轻链和重链一样，α-链和β-链都由可变区和恒定区组成[16 - 18]。分子克隆表明，β-链在进化上与免疫球蛋白相关，分别编码v（可变）、D（多样性）、J（连接）和c（恒定）片段，这些片段在T细胞中重排产生功能基因19 - 21,24 - 27。我们在此报道了编码人t细胞白血病HPB-MLT受体α-链的cDNA克隆。利用这些cDNA探针，我们发现α-链mRNA的表达和α-链v基因片段的重排仅发生在T细胞中。这些cdna预测的蛋白序列与t细胞受体β链和免疫球蛋白重链和轻链同源，特别是在vandj段。
The T-cell receptor has been studied intensely over the past 10 years in an effort to understand the molecular basis for major histocompatibility complex (MHC) restricted antigen recognition1–9. The use of anti-receptor monoclonal antibodies to isolate and characterize the receptor from human and murine T-cell clones10–15has shown that the protein consists of two disulphide-linked glycopeptides,αandβ, distinct from known immunoglobulin light and heavy chains. Like immunoglobulin light and heavy chains, however, both theα- andβ-chains are composed of variable and constant regions16–18. Molecular cloning has revealed19–23that theβ-chain is evolutionarily related to immunoglobulins, and is encoded in separateV(variable),D(diversity),J(joining) andC(constant) segments that are rearranged in T cells to produce a functional gene19–21,24–27. We report here cDNA clones encoding theα-chain of the receptor of the human T-cell leukaemia line HPB-MLT. Using these cDNA probes, we find that expression ofα-chain mRNA and rearrangement of anα-chainV-gene segment occur only in T cells. The protein sequence predicted by these cDNAs is homologous to T-cell receptorβ-chains and to immunoglobulin heavy and light chains, particularly in theVandJsegments.