Spatial approximation between a photolabile residue in position 13 of secretin and the amino terminus of the secretin receptor.

@article{Zang2003SpatialAB,
  title={Spatial approximation between a photolabile residue in position 13 of secretin and the amino terminus of the secretin receptor.},
  author={Mengwei Zang and Maoqing Dong and Delia I. Pinon and X Q Ding and Elizabeth M. Hadac and Zhijun Li and Terry P. Lybrand and Laurence J. Miller},
  journal={Molecular pharmacology},
  year={2003},
  volume={63 5},
  pages={993-1001}
}
The amino-terminal domain of class B G protein-coupled receptors is critically important for natural peptide agonist binding and action. The precise role it plays and the molecular basis of the interaction between ligand and this domain are not well understood. In the current work, we have developed a new probe for affinity labeling the secretin receptor through a photolabile benzoyl-phenylalanine residue in position 13. This represented a high affinity ligand (K(i) = 56 +/- 8 nM) that was a… CONTINUE READING
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A new approach to protein fold recognition

  • DT Jones, WR Taylor, JM Thornton
  • Nature (Lond)
  • 1992
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