T-CELL RECEPTOR-MHC CLASS-I PEPTIDE INTERACTIONS - AFFINITY, KINETICS, AND SPECIFICITY
T-CELL RECEPTOR-MHC CLASS-I PEPTIDE INTERACTIONS - AFFINITY, KINETICS, AND SPECIFICITY
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DOI：
10.1126/science.8052850
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发表时间：
1994-08-12
期刊：
影响因子：
56.9
通讯作者：
MARGULIES, DH
中科院分区：
文献类型：
--
作者：
CORR, M;SLANETZ, AE;MARGULIES, DH
携带α β T细胞受体（TCR）的T淋巴细胞活化中的关键区别事件是它们与分子复合物的相互作用，所述分子复合物由与抗原呈递细胞表面上的主要组织相容性复合物（MHC）编码的I类或II类分子结合的肽组成。在基于表面等离子体共振的直接实时测定中，测量纯化的TCR与鼠MHC I类分子H-2L（d）（sH-2L（d））的纯化的可溶性类似物和合成的八聚体肽p2CL的分子复合物的结合动力学。MHC-肽复合物从TCR上的动力学解离速率很快（2.6 × 10（-2）秒（-1），对应于约27秒的解离半衰期），动力学结合速率为2.1 × 10（5）M（-1）秒（-1）。解离平衡常数约为10（-7）M。这些值表明TCR必须与MHC-肽复合物的多价阵列相互作用以触发T细胞信号传导。
The critical discriminatory event in the activation of T lymphocytes bearing alpha beta T cell receptors (TCRs) is their interaction with a molecular complex consisting of a peptide bound to a major histocompatibility complex (MHC)-encoded class I or class II molecule on the surface of an antigen-presenting cell. The kinetics of binding were measured of a purified TCR to molecular complexes of a purified soluble analog of the murine MHC class I molecule H-2L(d) (sH-2L(d)) and a synthetic octamer peptide p2CL in a direct, real-time assay based on surface plasmon resonance. The kinetic dissociation rate of the MHC-peptide complex from the TCR was rapid (2.6 x 10(-2) second(-1), corresponding to a half-time for dissociation of approximately 27 seconds), and the kinetic association rate was 2.1 x 10(5) M(-1) second(-1). The equilibrium constant for dissociation was approximately 10(-7) M. These values indicate that TCRs must interact with a multivalent array of MHC-peptide complexes to trigger T cell signaling.