Natural agonist enhancing bis-His zinc-site in transmembrane segment V of the tachykinin NK3 receptor

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Standard

Natural agonist enhancing bis-His zinc-site in transmembrane segment V of the tachykinin NK3 receptor. / Rosenkilde, M M; Lucibello, M; Holst, B; Schwartz, T W.

In: FEBS Letters, Vol. 439, No. 1-2, 1998, p. 35-40.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Rosenkilde, MM, Lucibello, M, Holst, B & Schwartz, TW 1998, 'Natural agonist enhancing bis-His zinc-site in transmembrane segment V of the tachykinin NK3 receptor', FEBS Letters, vol. 439, no. 1-2, pp. 35-40.

APA

Rosenkilde, M. M., Lucibello, M., Holst, B., & Schwartz, T. W. (1998). Natural agonist enhancing bis-His zinc-site in transmembrane segment V of the tachykinin NK3 receptor. FEBS Letters, 439(1-2), 35-40.

Vancouver

Rosenkilde MM, Lucibello M, Holst B, Schwartz TW. Natural agonist enhancing bis-His zinc-site in transmembrane segment V of the tachykinin NK3 receptor. FEBS Letters. 1998;439(1-2):35-40.

Author

Rosenkilde, M M ; Lucibello, M ; Holst, B ; Schwartz, T W. / Natural agonist enhancing bis-His zinc-site in transmembrane segment V of the tachykinin NK3 receptor. In: FEBS Letters. 1998 ; Vol. 439, No. 1-2. pp. 35-40.

Bibtex

@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",

}

RIS

TY - JOUR

T1 - Natural agonist enhancing bis-His zinc-site in transmembrane segment V of the tachykinin NK3 receptor

AU - Rosenkilde, M M

AU - Lucibello, M

AU - Holst, B

AU - Schwartz, T W

N1 - Keywords: Amino Acid Sequence; Animals; Binding, Competitive; COS Cells; Histidine; Humans; Membrane Proteins; Molecular Sequence Data; Mutation; Neurokinin B; Protein Conformation; Receptors, Tachykinin; Zinc

PY - 1998

Y1 - 1998

N2 - 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.

AB - 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.

M3 - Journal article

C2 - 9849872

VL - 439

SP - 35

EP - 40

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 1-2

ER -

ID: 10536610