Title : Distinct domains of IFNalpha mediate immune and analgesic effects respectively.

Pub. Date : 2000 Aug 1

PMID : 10900338






4 Functional Relationships(s)
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1 After the 129th Tyr residue of human IFNalpha was mutated to Ser, the antiviral activity almost disappeared, but there still remained a strong analgesic activity that could be blocked by naloxone. Tyrosine interferon alpha 1 Homo sapiens
2 However, although the antiviral activity of IFNalpha decreased to 34.1% of wild type IFNalpha after the 122nd Tyr residue was changed to Ser, the analgesic activity of this mutant was lost completely. Tyrosine interferon alpha 1 Homo sapiens
3 However, although the antiviral activity of IFNalpha decreased to 34.1% of wild type IFNalpha after the 122nd Tyr residue was changed to Ser, the analgesic activity of this mutant was lost completely. Tyrosine interferon alpha 1 Homo sapiens
4 These studies show strong structural and functional similarities between INFalpha and opioid peptides, and inferred that the analgesic domain locates around the 122nd Tyr residue of IFNalpha molecule in tertiary structure. Tyrosine interferon alpha 1 Homo sapiens