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. Author manuscript; available in PMC: 2012 Apr 19.
Published in final edited form as: Biochemistry. 2011 Mar 29;50(15):3181–3192. doi: 10.1021/bi1019622

Table 1.

RGS specificity for inhibition of Gα/RGS binding.

RGS IC50 (μM) ± SEM Hill Slope
RGS4 wild Type 0.030 ± 0.006 −1.53
RGS4Cys−* N/A N/A
RGS7 N/A N/A
RGS8 11 ± 2 −0.99
RGS16 3.5 ± 2.4 −1.33
RGS19 0.12 ± 0.02 −0.61

IC50 values in the FCPIA assay show that CCG-50014 is >40 fold more potent for RGS4 than other RGS proteins. Data are presented as: mean IC50 values ± SEM from at least three independent experiments (for RGS4 and RGS8, n >28). N/A: No inhibition below the aqueous solubility limit of the compound (~200 μM).

*

RGS4Cys− is a mutated form of RGS that contains no cysteine residues in the RGS homology domain (13).