Wang Y X, Cui G Y, Shen J, Huang A J, Liu X Y, Chen Y Z, Jiang C L
Department of Neurobiology, Institute of Neuroscience, China Medical University, Shenyang, PR China.
Neuroreport. 2001 Mar 26;12(4):857-9. doi: 10.1097/00001756-200103260-00046.
Interferon-alpha (IFNalpha) is not only an immunoregulatory factor, but is also an analgesic molecule. We ever reported that there exist distinct domains in IFNalpha molecule that mediate immune and analgesic effects respectively and inferred that the analgesic domain locates around the 122nd Tyr residue of IFNalpha molecule in the tertiary structure. After the 36th Phe residue, which was located closely to the 122nd Tyr residue in the tertiary structure, was mutated to Ser using site-directed mutagenesis, the analgesic activity of this mutant lost completely, but the antiviral activity of IFNalpha still maintained 40.5% of wild type IFNalpha. The results suggest that the 36th Phe residue is one of the constituent for the analgesic domain of IFNalpha and inferred that the analgesic domain of IFNalpha consists of the 122nd Tyr and the residues around the 122nd in the tertiary structure, which include the 36th Phe.
α-干扰素(IFNα)不仅是一种免疫调节因子,也是一种镇痛分子。我们曾报道,IFNα分子中存在分别介导免疫和镇痛作用的不同结构域,并推测在三级结构中,镇痛结构域位于IFNα分子第122位酪氨酸残基附近。利用定点诱变技术将在三级结构中与第122位酪氨酸残基紧邻的第36位苯丙氨酸残基突变为丝氨酸后,该突变体的镇痛活性完全丧失,但IFNα的抗病毒活性仍维持在野生型IFNα的40.5%。结果表明,第36位苯丙氨酸残基是IFNα镇痛结构域的组成部分之一,并推测IFNα的镇痛结构域由三级结构中的第122位酪氨酸残基及其周围包括第36位苯丙氨酸在内的残基组成。