Identification of a direct interaction between interleukin 2 and the p64 interleukin 2 receptor gamma chain.
Identification of a direct interaction between interleukin 2 and the p64 interleukin 2 receptor gamma chain.
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鉴定白细胞介素 2 和 p64 白细胞介素 2 受体 γ 链之间的直接相互作用。
DOI：
10.1073/pnas.90.6.2428
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发表时间：
1993
影响因子：
11.1
通讯作者：
Robb,RJ
中科院分区：
文献类型：
--
作者：
Voss,SD;Leary,TP;Sondel,PM;Robb,RJ
白细胞介素2受体（IL-2 R）由至少两个亚基α和β组成，这两个亚基都可以结合白细胞介素2（IL-2）。最近的研究已经证明存在第三个亚基，称为IL-2 R γ链的64-kDa分子，并且已经表明γ链的功能是调节IL-2从受体解离的速率。在本报告中，我们已经解决了γ链是否调节IL-2 R亲和力的IL-2结合的贡献接触网站。使用允许IL-2 R复合物通过IL-2分子本身免疫沉淀的试剂，我们证明了稳定的IL-2-IL-2 R γ链复合物的存在。因此，这些研究确定IL-2 R γ链直接有助于IL-2结合位点，这与γ链通过其与IL-2的直接相互作用影响IL-2 R亲和力的假设一致。
The interleukin 2 receptor (IL-2R) consists of at least two subunits, alpha and beta, both of which can bind interleukin 2 (IL-2). Recent studies have demonstrated the existence of a third subunit, a 64-kDa molecule termed IL-2R gamma chain, and have suggested that gamma chain functions to regulate the rate of IL-2 dissociation from the receptor. In the present report we have addressed whether the gamma chain modulates IL-2R affinity by contributing contact sites for IL-2 binding. Using reagents that allow the IL-2R complex to be immunoprecipitated through the IL-2 molecule itself, we demonstrate the existence of a stable IL-2-IL-2R gamma-chain complex. These studies thus establish that the IL-2R gamma chain directly contributes to the IL-2-binding site, consistent with the hypothesis that gamma chain influences IL-2R affinity through its direct interaction with IL-2.