Peptide agonist docking in the N-terminal ectodomain of a class II G protein-coupled receptor, the VPAC1 receptor. Photoaffinity, NMR, and molecular modeling.

@article{Tan2006PeptideAD,
  title={Peptide agonist docking in the N-terminal ectodomain of a class II G protein-coupled receptor, the VPAC1 receptor. Photoaffinity, NMR, and molecular modeling.},
  author={Y Tan and Alain Couvineau and Samuel Murail and Emilie Ceraudo and J Neumann and Jean Jacques Lacap{\`e}re and Marc Laburthe},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 18},
  pages={12792-8}
}
The neuropeptide vasoactive intestinal peptide (VIP) strongly impacts on human pathophysiology and does so through interaction with class II G protein-coupled receptors named VIP pituitary adenylate cyclase-activating peptide (PACAP) receptors (VPACs). The molecular nature of VIP binding to receptors remains elusive. In this work, we have docked VIP in the human VPAC1 receptor by the following approach. (i) VIP probes containing photolabile residues in positions 6, 22, and 24 of VIP were used… CONTINUE READING

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