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Functional studies have suggested interactions with the nuclear export protein CRM1 [ 50], although direct binding interactions were not demonstrated in that study.
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This is possibly because the Ras Cdc25 binding interactions are not multilayered.
The free energy of the binding interaction is not sufficient to pull the unfolded monomer into a folded bound form.
EMSA using 212 300 and the PRC2 3m complex showed a similar affinity to that found for EZH2-EED binding (Kd = 111 ± 10 nM for PRC2 vs 135 ± 20 nM for EZH2-EED), indicating that the binding interaction was not an artifact arising from the more minimal EZH2-EED heterodimer.
All together, we conclude that other factors such as the hormone ligand and the tertiary structure of the NR are crucial players in cofactor binding, and that the contextual interactions are not as important as for other families.
Considering that the structure and function of a protein are generally determined by its component domains, we proposed a novel computational approach to predict drug targets supposing that drug-protein interactions are dominated by drug-domain interactions even if the drug-domain interactions are not necessarily physical binding interactions [ 32].
However, given that the first acidic region, STDE, of hTFIIEα has no effect on the binding, the interaction is not merely based on electrostatic interactions.
In the case that an interaction did not have at least one DNA binding domain, this interaction was not considered.
However, whether BAK1 acts as a regulator or co-receptor of BRI1 and how BR binding promotes BRI1-BAK1 interareionotre not well understood.
A reliable calculation of the binding affinity for this interaction was not possible because saturation of GST-IgFLNa20 21 GST-IgFLNa20 21ould not bindingeved.
pH drop had no effect on CusA binding to Ni2+, confirming that the interaction is not mediated by histidine but rather by methionine as it has been previously proposed [5].
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