The antiparallel pancreatic polypeptide fold in the binding of neuropeptide Y to Y1 and Y2 receptors.

@article{Fuhlendorff1990TheAP,
  title={The antiparallel pancreatic polypeptide fold in the binding of neuropeptide Y to Y1 and Y2 receptors.},
  author={Jens Fuhlendorff and Nils Langeland Johansen and S. G. Melberg and Henning Th\ogersen and Thue W. Schwartz},
  journal={The Journal of biological chemistry},
  year={1990},
  volume={265 20},
  pages={11706-12}
}
Neuropeptide Y (NPY) belongs to the pancreatic polypeptide fold (PP-fold) family of regulatory peptides. Analysis of circular dicroic spectra of NPY showed that it has a high degree of secondary structure in aqueous solution which is in agreement with the globular, folded crystal structure of PP. Using three different approaches with synthetic peptides, we have probed the importance of the PP-fold structure in the interaction of NPY with two types of binding sites, Y1 and Y2 receptors. First… CONTINUE READING

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