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

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 Abstract: 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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Language(s): eng - English
 Dates: 1995-06-092002-05-251995-07-17
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1006/bbrc.1995.2021
PMID: 7626082
 Degree: -

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Title: Biochemical and Biophysical Research Communications
  Other : Biochem. Biophys. Res. Commun.
Source Genre: Journal
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Publ. Info: Orlando, Fla. : Academic Press
Pages: - Volume / Issue: 212 (2) Sequence Number: - Start / End Page: 673 - 680 Identifier: ISSN: 0006-291X
CoNE: https://pure.mpg.de/cone/journals/resource/954922652205_1