The analgesic domain of IL-2

Yan Wang, Li Li, Jianfeng Liu, Zhiyong Wang, Chunlei Jiang, Xinyuan Liu

Research output: Contribution to journalArticlepeer-review

18 Scopus citations


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 were essential. These four residues are located close together at the tertiary structure level of IL-2.

Original languageEnglish (US)
Pages (from-to)542-545
Number of pages4
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - Jan 23 1997

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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