Casorati G, Traunecker A, Karjalainen K
Basel Institute for Immunology, Switzerland.
Eur J Immunol. 1993 Feb;23(2):586-9. doi: 10.1002/eji.1830230246.
In order to assess the structural independence of the T cell receptor (TCR) combining site from the rest of the molecule we have generated two recombinant chains consisting of a TCR V-J alpha region linked to the C beta and a TCR V-J beta linked to the C alpha. If the V and C domains of the TCR form independent domains, as has been shown for the Ig molecules, we would expect to obtain a functional chimeric TCR. Interestingly, it was found that the shuffled molecules are produced intracellularly in T cell hybridomas, but are not expressed on the cell surface. To explain this failure of the shuffled molecules we propose that the TCR has a more compact structure, compared to the Ig, and that it is indispensable to keep a longitudinal inter-domain contact between the V-J and C portion to have a functional molecule.
为了评估T细胞受体（TCR）结合位点相对于分子其余部分的结构独立性，我们构建了两条重组链，一条由与Cβ相连的TCR V-Jα区域组成，另一条由与Cα相连的TCR V-Jβ组成。如果TCR的V区和C区如Ig分子那样形成独立结构域，我们预期会获得功能性嵌合TCR。有趣的是，发现重排后的分子在T细胞杂交瘤细胞内产生，但未在细胞表面表达。为了解释重排分子的这种失败情况，我们提出，与Ig相比，TCR具有更紧密的结构，并且V-J部分和C部分之间保持纵向结构域间接触对于获得功能性分子是必不可少的。
