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. Author manuscript; available in PMC: 2012 Jan 1.
Published in final edited form as: Neuropharmacology. 2010 Jun 15;60(1):126–134. doi: 10.1016/j.neuropharm.2010.06.002

Figure 1.

Figure 1

Structures and binding assays for GluK1 competitive antagonists. (A) UBP315 and UBP318 are willardiine derivatives with bromine substitutions on the thiophene and uracil rings respectively; LY466195 is a decahydroisoquinoline with fluorine substitutions on the pyrrolidine ring. (B) Radioligand displacement curves for the purified GluK1 ligand binding domain showing competition between 3[H]-L-glutamate and three antagonists, fit with single binding site isotherms of 33 ± 4 nM, 186 ± 23 nM and 38 ± 7 nM for UBP315, UBP318 and LY466195, respectively; values are mean ± SEM of triplicate measurements.