Meanwhile, the rescuing of the binding affinity implies that a preordered IKK-binding region of NEMO is compatible with IKK binding, and the conformational heterogeneity observed in NEMO(44 111) may be an artifact of the truncation.
This decreased affinity implies that binding of CpxI(47-134) to SCΔ60 is not saturated upon addition of 1.5 equivalents of CpxI(47-134) (arrow in Figure 4B).
Based on our results, which demonstrate that the CpG and non-CpG PS DNA have the same stoichiometry with TLR9 but with different binding affinity, it implies that the CpG and non CpG DNA might bind to different sites of TLR9.
The conservation of the relative affinities implies that the binding preferences of the subtypes will not by themselves determine the heterogeneous distribution of some subtypes in cell nuclei, as high and lower affinity chromatin binding sites should be occupied with similar probabilities by the different subtypes.
Accordingly, self-affinity implies that the fault surface appears smoother as the spatial scale increases.
In the absence of the Ubl domain, the L266K mutation did not further increase the affinity of pUb binding, implying that the enhanced affinity observed with the L266K and N273K mutants was linked to the release of the Ubl domain (Figs 3A and EV3A).
For binding to Fc, the longest n = 6 linker gave the highest affinity, implying longer interchain distance between the two binding sites.
For a series of structurally related agonists, there is a correlation between the energies of low- and high-affinity binding, which implies that gating commences with the formation of the low-affinity complex.
As only AtACBP6 responds to freezing stress [ 39, 53], the stronger binding affinity of rAtACBP6 to long-chain acyl-CoA esters may imply that tight acyl-lipid binding becomes more critical under stress conditions than AtACBP4 and AtACBP5.
Mutations that reduce CD44- and Par3-binding affinity do not affect on PI 3, 4, 5 P3-binding affinity (Supplementary Figure S9A), implying that the PHCCEx domain binds PIs and proteins with no significant interference or cooperativity.
