The analgesic domain of IL-2

被引:17
|
作者
Wang, Y [1 ]
Li, L [1 ]
Liu, JF [1 ]
Wang, ZY [1 ]
Jiang, CL [1 ]
Liu, XY [1 ]
机构
[1] CHINESE ACAD SCI,SHANGHAI INST BIOCHEM,SHANGHAI 200031,PEOPLES R CHINA
关键词
D O I
10.1006/bbrc.1996.5961
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Human recombinant interleukin-2 (IL-2) has been showed to exert an analgesic effect and some experiments suggested that opioid receptors were involved. Because the aromatic residues at the N-termini of opioid peptides are crucial for their binding to the opioid receptors, all nine aromatic residues in IL-2 were mutated by site-directed mutagenesis and both the analgesic activity and the immune activity of the wild-type and mutated IL-2 were tested, The result indicated that there exists a putative analgesic function domain in IL-2, in which Phe44, Tyr45, Tyr107, and Phe117 mere essential. These four residues are located close together at the tertiary structure level of IL-2. (C) 1997 Academic Press.
引用
收藏
页码:542 / 545
页数:4
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