Nishimura C, Futatsugi K, Yasukawa K, Kishimoto T, Arata Y
Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
FEBS Lett. 1991 Apr 9;281(1-2):167-9. doi: 10.1016/0014-5793(91)80384-f.
Amino acid substitutions of human interleukin-6 (IL-6) were performed. Single substitution Met162----Ala and double substitutions Leu159.166----Val resulted in a significant decrease of IL-6 activity in the production of immunoglobulin (Ig) from B-cells. Single substitution Leu166----Val or Leu159----Val gave a slight or no significant decrease in the Ig-induction activity, respectively. The receptor-binding activity of each IL-6 mutant was also examined. It was observed that the decrease of the receptor-binding activity was generally in parallel with that of the Ig-induction activity. We therefore suggest that hydrophobic side-chains existing in Met162, Leu159, and Leu166 are significantly involved in the receptor-binding of IL-6.
对人白细胞介素-6（IL-6）进行了氨基酸替换。单替换Met162----Ala以及双替换Leu159.166----Val导致B细胞产生免疫球蛋白（Ig）时IL-6活性显著降低。单替换Leu166----Val或Leu159----Val分别使Ig诱导活性略有降低或无显著降低。还检测了每个IL-6突变体的受体结合活性。观察到受体结合活性的降低通常与Ig诱导活性的降低平行。因此，我们认为存在于Met162、Leu159和Leu166中的疏水侧链与IL-6的受体结合密切相关。
