Allosteric modulation, thermodynamics and binding to wild‐type and mutant (T277A) adenosine A1 receptors of LUF5831, a novel nonadenosine‐like agonist

  title={Allosteric modulation, thermodynamics and binding to wild‐type and mutant (T277A) adenosine A1 receptors of LUF5831, a novel nonadenosine‐like agonist},
  author={Laura H. Heitman and Thea Mulder-Krieger and Ronald F Spanjersberg and Jacobien K. von Frijtag Drabbe K{\"u}nzel and Alessandro Dalpiaz and Adriaan P. IJzerman},
  journal={British Journal of Pharmacology},
The interaction of a new nonribose ligand (LUF5831) with the human adenosine A1 receptor was investigated in the present study. Radioligand binding experiments were performed in the absence and presence of diverse allosteric modulators on both wild‐type (wt) and mutant (T277A) adenosine A1 receptors. Thermodynamic data were obtained by performing these assays at different temperatures. In addition, cyclic adenosine monophosphate (cAMP) assays were performed. The presence of allosteric… 
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The binding-site crevice of the D4 dopamine receptor is coupled to three distinct sites of allosteric modulation.
  • J. SchetzD. Sibley
  • Biology, Chemistry
    The Journal of pharmacology and experimental therapeutics
  • 2001
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