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. Author manuscript; available in PMC: 2018 Oct 18.
Published in final edited form as: Nature. 2018 Apr 18;556(7702):520–524. doi: 10.1038/s41586-018-0046-x

Extended Data Table 3.

Binding of Y1R antagonists and agonists to membrane preparations from Sf9 cells expressing wild-type and mutant Y1Rs

a. Binding of antagonists to wild-type and mutant Y1Rs
Y1R mutants Kd (nM)* Ki (nM)
[3H]-UR-MK299 n BMS-193885 n BIBP3226 n BIBO3304 n UR-MK136 n UR-MK289 n
Wild type 0.17 ± 0.03 3 22 ± 6 3 2.4; 3.1 2 1.6 ± 0.3 3 2.8; 4.0 2 25; 28 2
Crystallization construct 0.33 ± 0.06 3 38 ± 2 4 / / / /
C1213.33A 1.4; 2.4 2 / / / / /
I1243.36A 7.0; 8.0 2 9,500 ± 1,700 3 15 ± 5 3 11 ± 2 3 12 ± 2 3 80 ± 16 3
I1243.36F 1.3; 1.9 2 / / / / /
F1734.60A 9.1 ± 2.2 4 590 ± 220 3 68; 84 2 120 ± 17 4 88; 110 2 660 ± 110§ 5
F1734.60W 0.31; 0.32 2 110; 130 2 15; 26 2 13 ± 4 3 3.6; 4.3 2 6.8; 9.2 2
T2125.39A 0.12; 0.18 2 150; 150 2 13; 12 2 2.5 ± 0.3 3 5.7; 7.5 2 18; 21 2
L2155.42G 4.2; 5.6 2 9.6 ± 1.9 4 43; 23 2 47 ± 4 3 11; 8.4 2 29; 30 2
Q2195.46A 4.1; 5.1 2 0.50 ± 0.07 4 35; 53 2 6.2 ± 0.7 3 16 ± 4 3 13 ± 4 3
Q2195.46V 5.1 ± 1.2 3 / / / / /
W2766.48A >500 3 / / / / /
L2796.51A 1.0; 1.1 2 160; 220 2 110; 110 2 13 ± 2 3 120; 150 2 320 ± 40 3
T2806.52A 0.16 ± 0.04 3 7,300 ± 1,300 3 32 ± 7 3 2.6 ± 0.4 3 4.2 ± 1.1 3 8.2 ± 4.2 3
N2836.55A >500; >500 2 / / / / /
D2876.59A >500; >500 2 / / / / /
F3027.35A >500; >500 2 / / / / /
b. Binding of NPYs to wild-type Y1R
Kd (nM)* Ki (nM)
Y1R [3H]-UR-MK299 n Human NPY n Porcine NPY n
Wild type 0.89; 1.1 2 4.1; 4.2 2 2.8 ± 0.4 4
*

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) (Note: the sodium-free buffer was used for the determination of agonist binding affinity because porcine NPY exhibited approx. 10-fold higher affinity in the sodium-free buffer compared to the sodium-containing buffer (data not shown)).

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).

Sample size, the number of independent experiments performed in technical triplicate. If n>2, data are shown as means ± s.e.m. If n=2, results of two individual experiments are shown.

§

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 different from zero (P < 0.005, one-sample one-tailed t-test), which is indicative of a non-competitive mechanism.

/: not tested.