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

@article{Cao1995TheAF,
  title={The amino-terminal fragment of the adenylate cyclase activating polypeptide (PACAP) receptor functions as a high affinity PACAP binding domain.},
  author={Yudong Cao and Gerald Gimpl and Falk Fahrenholz},
  journal={Biochemical and biophysical research communications},
  year={1995},
  volume={212 2},
  pages={
          673-80
        }
}
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… CONTINUE READING
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