The development of immune-modulate molecule using the binding specificity of Toll-Interleukin-1 receptor domain

在这项研究中，我们的目标是开发的分子，它调节Toll-白细胞介素-1受体（TIR）信号转导使用的TIR域的结合特异性MyD 88。用E.大肠杆菌蛋白表达系统。为了稳定该蛋白，MyD 88的两个半胱氨酸氨基酸C203和C280突变为丝氨酸（CS）。PTD-MyD 88-DN-CS蛋白引起NF-κ B转录活性的非配体依赖性增加。

In this study, we aimed the development of the molecule, which modulates the Toll-Interleukin-1 receptor (TIR) signaling using the binding specificity of TIR domain of MyD88. The dominant negative form (DN) of MyD88 fused with protein transduction domain (PTD) was purified with E. Coli protein expression system. In order to stabilize this protein, two cysteine amino acids of MyD88, C203 and C280, were mutated to serine (CS). PTD-MyD88-DN-CS protein caused the ligand-independent increase of transcriptional activity of NF-kappaB.