Binding specificity of multiprotein signaling complexes is determined by both cooperative interactions and affinity preference
Binding specificity of multiprotein signaling complexes is determined by both cooperative interactions and affinity preference
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DOI：
10.1021/bi0357311
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发表时间：
2004-04-13
期刊：
影响因子：
2.9
通讯作者：
Samelson, LE
中科院分区：
文献类型：
--
作者：
Houtman, JCD;Higashimoto, Y;Samelson, LE
多蛋白复合物在受体和转接器蛋白的产生对细胞内信号通路的激活至关重要。在这项研究中，我们使用了多种生化和生物物理方法来研究几种含有SH2和SH3结构域的信号蛋白的结合特性，因为它们与t细胞活化（LAT）的适配器蛋白连接物相互作用，形成多蛋白复合物。我们观察到，这些蛋白质对各种LAT酪氨酸的结合特异性似乎受到结合亲和力和蛋白质-蛋白质合作相互作用的限制。这些研究提供了关于不同结合参数如何决定多蛋白信号复合物体内结合位点特异性的定量信息。
The generation of multiprotein complexes at receptors and adapter proteins is crucial for the activation of intracellular signaling pathways. In this study, we used multiple biochemical and biophysical methods to examine the binding properties of several SH2 and SH3 domain-containing signaling proteins as they interact with the adapter protein linker for activation of T-cells (LAT) to form multiprotein complexes. We observed that the binding specificity of these proteins for various LAT tyrosines appears to be constrained both by the affinity of binding and by cooperative protein-protein interactions. These studies provide quantitative information on how different binding parameters can determine in vivo binding site specificity observed for multiprotein signaling complexes.