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. Author manuscript; available in PMC: 2010 Aug 2.
Published in final edited form as: Biochemistry. 2006 Aug 1;45(30):9074–9084. doi: 10.1021/bi060567d

Table 1.

Equilibrium dissociation constants for interaction of nucleotides with PKR.a

Nucleotide Enzyme Form
Unphosphorylated Phosphorylated K296R Mutant Unphos. + 40mer dsRNA
mant-AMPPNP 33.8 ± 0.7b
34.8 ± 3.6c
34.0 ± 0.7b 11.5 ± 0.3b 102.3 ± 3.6c
mant-ATP - 24.6 ± 1.7c 10.3 ± 0.8b -
ATP - 24.4 ± 0.1d 20.2 ± 1.7d -
AMPPNP 97.7 ± 1.7d 34.0 ± 0.1d 22.8 ± 2.0d 160.5 ± 1.4d
ADP 76.5 ± 1.1d 11.6 ± 0.7d 12.5 ± 0.3d 67.0 ± 0.7d
a

Kd values in units of μM.

b

Forward anisotropy titration.

c

Reverse anisotropy titration.

d

Competition titration using mant-AMPPNP.