Fig. 4: In vitro characterization of pAp. | Communications Biology

Fig. 4: In vitro characterization of pAp.

From: Characterization of exoribonuclease XRN1 as a cancer target and identification of adenosine-3’,5’-bisphosphate as a potent enzyme inhibitor

Fig. 4: In vitro characterization of pAp.

a Chemical structure of pAp. b pAp is an inhibitor of hXRN1 (IC50 = 36 ± 10 nM). Error bars represent standard deviation of 6 replicates. pAp binds to c hXRN1-Avi (KD = 12 ± 1 nM) and d hXRN2-Avi (KD = 14 ± 4 nM). e pAp does not bind to the metal-binding site mutant hXRN1-D208A-Avi. f pAp IC50 curves shift right with increasing amounts of RNA substrate. Error bars represent standard deviation of 2 replicates. g The near-linear increases in pAp IC50 values as RNA concentration is increased (α = 23) is indicative of a mixed-competitive mechanism with the oligonucleotide substrate.

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