Richardson N E, Chang H C, Brown N R, Hussey R E, Sayre P H, Reinherz E L
Laboratory of Immunobiology, Dana-Farber Cancer Institute, Boston, MA.
Proc Natl Acad Sci U S A. 1988 Jul;85(14):5176-80. doi: 10.1073/pnas.85.14.5176.
The 50-kDa T11 (CD2) T-lymphocyte surface glycoprotein facilitates physical adhesion between T-lineage cells and their cognate cellular counterparts (cytotoxic T-lymphocytes-target cells, helper T lymphocytes-antigen-presenting cells, or thymocytes-thymic epithelium) as well as signaling through the antigen-specific T3-Ti receptor complex. To examine the relationship between the structure and function of the T11 molecule, we have utilized a baculoviral expression system to produce milligram quantities of the hydrophilic extracellular T11 segment. Enzyme cleavage, microsequencing, and HPLC analyses of the expressed protein in conjunction with genomic cloning information show that the domain involved in cellular adhesion is encoded by a single 321-base-pair exon.
50 kDa的T11（CD2）T淋巴细胞表面糖蛋白促进T系细胞与其同源细胞对应物（细胞毒性T淋巴细胞-靶细胞、辅助性T淋巴细胞-抗原呈递细胞或胸腺细胞-胸腺上皮细胞）之间的物理粘附，以及通过抗原特异性T3-Ti受体复合物进行信号传导。为了研究T11分子的结构与功能之间的关系，我们利用杆状病毒表达系统产生了毫克量的亲水性细胞外T11片段。对表达蛋白进行酶切、微量测序和高效液相色谱分析，并结合基因组克隆信息表明，参与细胞粘附的结构域由一个321个碱基对的外显子编码。
