Sayre P H, Chang H C, Hussey R E, Brown N R, Richardson N E, Spagnoli G, Clayton L K, Reinherz E L
Proc Natl Acad Sci U S A. 1987 May;84(9):2941-5. doi: 10.1073/pnas.84.9.2941.
The T11 (CD2) sheep-erythrocyte-binding protein is a T-cell surface molecule involved in activation of T lymphocytes and thymocytes, including those lacking the T3-Ti antigen-receptor complex. The primary structure of T11 was deduced from protein microsequencing and cDNA cloning. The mature human protein appears to be divided into three domains: a hydrophilic 185 amino acid external domain bearing only limited homology to the T-cell surface protein T4 and the immunoglobulin kappa light chain variable region, a 25 amino acid hydrophobic transmembrane segment, and a 126 amino acid cytoplasmic domain rich in prolines and basic residues. Transfection of cDNAs encoding either the 1.7- or the 1.3-kilobase T11 mRNA into COS-1 cells resulted in expression of surface T11 epitopes as well as sheep-erythrocyte-binding capacity. The predicted structure is consistent with the possibility that T11 functions in signal transduction.
T11（CD2）绵羊红细胞结合蛋白是一种T细胞表面分子，参与T淋巴细胞和胸腺细胞的激活，包括那些缺乏T3-Ti抗原受体复合物的细胞。T11的一级结构是通过蛋白质微量测序和cDNA克隆推导出来的。成熟的人蛋白质似乎分为三个结构域：一个亲水性的185个氨基酸的外部结构域，与T细胞表面蛋白T4和免疫球蛋白κ轻链可变区只有有限的同源性；一个25个氨基酸的疏水跨膜片段；以及一个富含脯氨酸和碱性残基的126个氨基酸的胞质结构域。将编码1.7或1.3千碱基T11 mRNA的cDNA转染到COS-1细胞中，导致表面T11表位的表达以及绵羊红细胞结合能力。预测的结构与T11在信号转导中起作用的可能性一致。
