Extended Data Table 3 Binding of Y1R antagonists and agonists to membrane preparations from Sf9 cells expressing wild-type and mutant Y1 receptors

From: Structural basis of ligand binding modes at the neuropeptide Y Y1 receptor

  1. *Dissociation constant determined by saturation binding at Sf9 membranes (receptor expression was confirmed by western blot analysis) using a sodium-containing buffer (a) or a sodium-free buffer (b) (the sodium-free buffer was used for the determination of agonist binding affinity because porcine NPY exhibited approximately tenfold higher affinity in the sodium-free buffer compared to the sodium-containing buffer (data not shown)).
  2. †Dissociation constant determined by competition binding with [3H]UR-MK299 at Sf9 membranes using a sodium-containing buffer (a) or a sodium-free buffer (b).
  3. ‡Sample size; the number of independent experiments performed in technical triplicate. If n > 2, data are shown as mean ± s.e.m. If n = 2, results of two individual experiments are shown.
  4. §The lower curve plateau of the four-parameter logistic fit, amounting to 17 ± 3% of specifically bound [3H]UR-MK299 (mean ± s.e.m. from five independent experiments), was significantly different from zero (P < 0.005, one-sample one-tailed t-test), which is indicative of a non-competitive mechanism.
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