Kersh E N, Shaw A S, Allen P M
Center for Immunology and Department of Pathology, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA.
Science. 1998 Jul 24;281(5376):572-5. doi: 10.1126/science.281.5376.572.
The T cell receptor (TCR) alphabeta heterodimer interacts with its ligands with high specificity, but surprisingly low affinity. The role of the zeta component of the murine TCR in contributing to the fidelity of antigen recognition was examined. With sequence-specific phosphotyrosine antibodies, it was found that zeta undergoes a series of ordered phosphorylation events upon TCR engagement. Completion of phosphorylation steps is dependent on the nature of the TCR ligand. Thus, the phosphorylation steps establish thresholds for T cell activation. This study documents the sophisticated molecular events that follow the engagement of a low-affinity receptor.
T细胞受体（TCR）αβ异二聚体与其配体相互作用时具有高度特异性，但亲和力却出奇地低。研究了小鼠TCR的ζ组分在提高抗原识别保真度方面的作用。使用序列特异性磷酸酪氨酸抗体发现，ζ在TCR结合后会经历一系列有序的磷酸化事件。磷酸化步骤的完成取决于TCR配体的性质。因此，磷酸化步骤为T细胞激活设定了阈值。这项研究记录了低亲和力受体结合后发生的复杂分子事件。
