Disruption of the Na+ ion binding site as a mechanism for positive allosteric modulation of the mu-opioid receptor.

@article{Livingston2014DisruptionOT,
  title={Disruption of the Na+ ion binding site as a mechanism for positive allosteric modulation of the mu-opioid receptor.},
  author={Kathryn E. Livingston and John R. Traynor},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2014},
  volume={111 51},
  pages={18369-74}
}
Positive allosteric modulation of the mu-opioid receptor (MOPr), the site of action of all clinically used opioids, represents a potential approach for the management of pain. We recently reported on positive allosteric modulators of MOPr (mu-PAMs), a class A G protein coupled receptor (GPCR). This study was designed to examine the mechanism of allostery by comparing the degree to which opioid ligand structure governs modulation. To do this we examined the interaction of the mu-PAM, BMS-986122… CONTINUE READING

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References

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Discovery of positive allosteric modulators and silent allosteric modulators of the μ-opioid receptor.

Proceedings of the National Academy of Sciences of the United States of America • 2013

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