Replacement of Gln280 by His in TM6 of the human ORL1 receptor increases affinity but reduces intrinsic activity of opioids.

@article{Mollereau1996ReplacementOG,
  title={Replacement of Gln280 by His in TM6 of the human ORL1 receptor increases affinity but reduces intrinsic activity of opioids.},
  author={Catherine Mollereau and Christiane Moisand and J L Butour and Marc Parmentier and J. C. Meunier},
  journal={FEBS letters},
  year={1996},
  volume={395 1},
  pages={17-21}
}
The ORL1 (Opioid Receptor-Like) receptor is the G protein-coupled receptor whose amino acid sequence is closest to those of opioid receptors. Residues that are conserved in ORL1 and the three types of opioid receptor, but also a residue, His in the sixth putative transmembrane (TM6) helix, which is present in all opioid receptor types but absent in ORL1, appear to play a key role in receptor recognition and/or activation. Here we have sought to create an opioid binding pocket in the non-opioid… CONTINUE READING

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