The analgesic domain of IL-2.
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.
Wang
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Y
Shanghai Institute of Biochemistry, Chinese Academy of Sciences, People's Republic of China.
Li
L
L
Liu
J
J
Wang
Z
Z
Jiang
C
C
Liu
X
X
D000700:Analgesics / Q000008:administration & dosage / Q000737:chemistry*; D000818:Animals; D006801:Humans; D007275:Injections, Intravenous; D007376:Interleukin-2 / Q000737:chemistry* / Q000235:genetics; D008297:Male; D016297:Mutagenesis, Site-Directed; D017288:Pain Threshold / Q000187:drug effects; D017434:Protein Structure, Tertiary; D051381:Rats; D017208:Rats, Wistar; D013329:Structure-Activity Relationship
D000700:Analgesics; D007376:Interleukin-2