@article{e927ff30fada11ddb219000ea68e967b,
title = "Natural agonist enhancing bis-His zinc-site in transmembrane segment V of the tachykinin NK3 receptor",
abstract = "In the wild-type tachykinin NK3A receptor histidyl residues are present at two positions in TM-V, V:01 and V:05, at which Zn2+ functions as an antagonist in NK1 and kappa-opioid receptors with engineered metal-ion sites. Surprisingly, in the NK3A receptor Zn2+ instead increased the binding of the agonist 125I-[MePhe7]neurokinin B to 150%. [MePhe7]neurokinin B bound to the NK3A receptor in a two-component mode of which Zn2+ eliminated the subnanomolar binding mode but induced a higher binding capacity of the nanomolar binding mode. Signal transduction was not induced by ZnCl2 but 10 microM ZnCl2 enhanced the effect of neurokinin B. Ala-substitution of HisV:01 eliminated the enhancing effect of Zn2+ on peptide binding. It is concluded that physiological concentrations of Zn2+ have a positive modulatory effect on the binding and function of neurokinin B on the NK3A receptor through a bis-His site in TM-V.",
author = "Rosenkilde, {M M} and M Lucibello and B Holst and Schwartz, {T W}",
note = "Keywords: Amino Acid Sequence; Animals; Binding, Competitive; COS Cells; Histidine; Humans; Membrane Proteins; Molecular Sequence Data; Mutation; Neurokinin B; Protein Conformation; Receptors, Tachykinin; Zinc",
year = "1998",
language = "English",
volume = "439",
pages = "35--40",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "1-2",
}