Spatial approximation between secretin residue five and the third extracellular loop of its receptor provides new insight into the molecular basis of natural agonist binding.

@article{Dong2008SpatialAB,
  title={Spatial approximation between secretin residue five and the third extracellular loop of its receptor provides new insight into the molecular basis of natural agonist binding.},
  author={Maoqing Dong and Polo H C Lam and Delia I. Pinon and Patrick M. Sexton and Ruben Abagyan and Laurence J. Miller},
  journal={Molecular pharmacology},
  year={2008},
  volume={74 2},
  pages={413-22}
}
The amino terminus of class II G protein-coupled receptors plays an important role in ligand binding and receptor activation. Understanding of the conformation of the amino-terminal domain of these receptors has been substantially advanced with the solution of nuclear magnetic resonance and crystal structures of this region of receptors for corticotrophin-releasing factor, pituitary adenylate cyclase-activating polypeptide, and gastric inhibitory polypeptide. However, the orientation of the… CONTINUE READING