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  The amino-terminal fragment of the adenylate cyclase activating polypeptide (PACAP) receptor functions as a high affinity PACAP binding domain

Cao, Y.-J., Gimpl, G., & Fahrenholz, F. (1995). The amino-terminal fragment of the adenylate cyclase activating polypeptide (PACAP) receptor functions as a high affinity PACAP binding domain. Biochemical and Biophysical Research Communications, 212(2), 673-680. doi:10.1006/bbrc.1995.2021.

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Datensatz-Permalink: https://hdl.handle.net/21.11116/0000-0008-0EDB-3 Versions-Permalink: https://hdl.handle.net/21.11116/0000-0008-0EDC-2
Genre: Zeitschriftenartikel

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 Urheber:
Cao, Yong-Jiang1, Autor           
Gimpl, Gerald1, Autor           
Fahrenholz, Falk1, Autor           
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              

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Schlagwörter: -
 Zusammenfassung: The PACAP receptor represents a member of a novel subfamily of G-protein coupled receptors with a common structurally conserved extracellular domain of about 150 amino acids. We have addressed the question whether this extracellular amino-terminus of the PACAP type I receptor can solely function as a PACAP binding domain. For that purpose a cDNA was constructed that encodes the membrane-anchored amino-terminus of the rat PACAP receptor including the decapeptide epitope EQKLISEEDL for immunodetection. COS-7 cells were transfected with this cDNA and a comparable construct of the wild-type receptor. Binding analysis showed that the amino-terminal fragment of the PACAP receptor bound PACAP with high-affinity (Kd = 3.8 nM; Bmax = 12.8 pmol/mg protein). In comparison to the full-length receptor (Kd = 0.2 nM; Bmax = 1.96 pmol/mg protein) its affinity was reduced by a factor of about 20. The results suggest that the amino-terminus of the PACAP receptor functions as the major binding site for its ligand.

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Sprache(n): eng - English
 Datum: 1995-06-092002-05-251995-07-17
 Publikationsstatus: Erschienen
 Seiten: 8
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1006/bbrc.1995.2021
PMID: 7626082
 Art des Abschluß: -

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Titel: Biochemical and Biophysical Research Communications
  Andere : Biochem. Biophys. Res. Commun.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: Orlando, Fla. : Academic Press
Seiten: - Band / Heft: 212 (2) Artikelnummer: - Start- / Endseite: 673 - 680 Identifikator: ISSN: 0006-291X
CoNE: https://pure.mpg.de/cone/journals/resource/954922652205_1