Parnes J R, Sizer K C, Sukhatme V P, Hunkapiller T
Behring Inst Mitt. 1985 Aug(77):48-55.
We have determined the primary structure of the Leu-2/T8 T lymphocyte differentiation antigen from the complete nucleotide sequence of a cDNA clone. The protein consists of a classical signal peptide, two external protein domains, a hydrophobic transmembrane segment, and a highly charged intracytoplasmic tail. The N-terminal external domain of the mature protein is homologous to immunoglobulin and T cell receptor variable regions. Protein structural predictions suggest that this domain can indeed fold like an immunoglobulin domain. The Leu-2/T8 protein has no segment that is homologous to a constant region. However, the membrane-proximal domain appears to serve as a hinge. These studies indicate that Leu-2/T8 is another member of the immunoglobulin supergene family.
我们已根据一个cDNA克隆的完整核苷酸序列确定了Leu-2/T8 T淋巴细胞分化抗原的一级结构。该蛋白质由一个典型的信号肽、两个细胞外蛋白质结构域、一个疏水跨膜片段和一个高度带电的胞质内尾部组成。成熟蛋白质的N端细胞外结构域与免疫球蛋白和T细胞受体可变区同源。蛋白质结构预测表明，该结构域确实可以折叠成免疫球蛋白结构域。Leu-2/T8蛋白没有与恒定区同源的片段。然而，膜近端结构域似乎起到了铰链的作用。这些研究表明，Leu-2/T8是免疫球蛋白超基因家族的另一个成员。
