Wang Y, Li L, Liu J, Wang Z, Jiang C, Liu X
Shanghai Institute of Biochemistry, Chinese Academy of Sciences, People's Republic of China.
Biochem Biophys Res Commun. 1997 Jan 23;230(3):542-5. doi: 10.1006/bbrc.1996.5961.
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, Tyrl07, and Phell7 were essential. These four residues are located close together at the tertiary structure level of IL-2.
人重组白细胞介素-2（IL-2）已被证明具有镇痛作用，一些实验表明这涉及阿片受体。由于阿片肽N端的芳香族残基对其与阿片受体的结合至关重要，通过定点诱变对IL-2中的所有九个芳香族残基进行了突变，并测试了野生型和突变型IL-2的镇痛活性和免疫活性。结果表明，IL-2中存在一个假定的镇痛功能域，其中苯丙氨酸44、酪氨酸45、酪氨酸107和苯丙氨酸117是必需的。这四个残基在IL-2的三级结构水平上靠得很近。
