TY - JOUR
T1 - The analgesic domain of IL-2
AU - Wang, Yan
AU - Li, Li
AU - Liu, Jianfeng
AU - Wang, Zhiyong
AU - Jiang, Chunlei
AU - Liu, Xinyuan
PY - 1997/1/23
Y1 - 1997/1/23
N2 - 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.
AB - 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.
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U2 - 10.1006/bbrc.1996.5961
DO - 10.1006/bbrc.1996.5961
M3 - Article
C2 - 9015358
AN - SCOPUS:0031584083
SN - 0006-291X
VL - 230
SP - 542
EP - 545
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -