. 2018 May 9;8:7381. doi: 10.1038/s41598-018-25765-2

Table 2.

Calculated equilibrium dissociation constants of MCPIP1 complexes with selected oligonucleotides.

	MCPIP1_D141N 1–599 aa K_d (nM)	PIN-ZF_D141N 134–327 aa K_d (nM)	PIN_D141N 134–297 aa K_d (nM)
Stem-loop RNAs
mIL-6_82–106 5′FAM	6.5 ± 2.1^a	6.6 ± 3.1^b	24.1 ± 7.3^ab
mIL-6_82–106 3′FAM	8.6 ± 2.6^a	4.8 ± 1.8^b	21.8 ± 6.3^ab
mIL-6_82–106 RS	9.8 ± 2.3^a	15.1 ± 7.3^b	39.3 ± 8.6^ab
mIL-6_82–106 YR	9.5 ± 5.2^a	14.4 ± 9.6	25.1 ± 7.0^a
mIL-6_85–101 short stem	9.2 ± 4.0^a	20 ± 10	20.7 ± 7.2^a
hIL-6_82–99	4.1 ± 3.6^a	13.2 ± 6.8	15.1 ± 4.5^a
consensus stem-loop	3.8 ± 2.8^a	9.1 ± 3.2^b	36 ± 17^ab
ssRNA
mIL-6_82–93	19 ± 11^a	34 ± 18	41 ± 12^a
mIL-6_82–88	14.5 ± 8.1^a	32 ± 20	40 ± 12^a
poly-U	14.8 ± 7.2^a	43 ± 23	39 ± 11^a
mIL-6_82–93 ssDNA	18.3 ± 8.2	36 ± 20	21.7 ± 6.6
mIL-6_82–93 dsDNA	118 ± 49	80 ± 30	56 ± 17

The analyzed proteins were mutated forms of MCPIP1 and its ribonuclease domain (MCPIP1_D141N, PIN-ZF_D141N, and PIN_D141N). K_d values were determined using DynaFit4 software with the implemented model of sequential binding of two proteins to a single oligonucleotide with a single dissociation constant. Errors are shown as standard deviations, n = 3. Statistical significance (P value < 0.05) between selected groups is shown by the following indexes: ^a and ^b for comparison of the MCPIP1_D141N with PIN_D141N and PIN-ZF_D141N with PIN_D141N groups, respectively. Differences observed between the MCPIP1_D141N and PIN-ZF_D141N groups are not statistically significant.