These were then evaluated to determine their ability to bind to the L11 binding domain of the prokaryotic ribosome and inhibit bacterial protein translation.
The sorted library IgGs and the serum IgGs bound weakly to the resurfaced Env gp120, RSC3, and did not bind to the CD4 binding site (CD4bs) knock-out mutant, ΔRSC3.
Computational docking studies allowed to predict that, like nutlin-3A (a well-known small-molecule inhibitor of p53 MDM2 interaction), chalcones 3 and 4 bind to the p53-binding site of MDM2.
In previous studies, all peptides were assumed to bind to the SH3 binding pocket in the canonical binding mode.
Nutlins bind to the p53-binding pocket in the MDM2 protein, thus inhibiting the binding of p53 and activating the p53 pathway in cancer cells with wild-type p53, including solid tumors [10], [11] and hematological malignancies [12], [13], [14], [15].
Dlg3 contains a central SH3 domain which could bind to the SH3 binding or PRR domain of Fltp.
In one case, Ca2+ ions bind to the Ca2+ binding site on the channel and thereby inhibit the channel's conductivity by direct interaction.
We were curious whether known TFs could bind to the SOX2 binding regions that we identified and act as SOX2 cooperators for the regulation of gene expression.
Although Sox2 does not respond to the reporter in RU cells, possibly due to the fact that Sox2 in RU cells cannot bind to the Sox2 binding motif present in the Sox2 reporter [ 39], Sox2 in RU cells can bind to the alternative Sox2 binding motif present in the Twist1 gene promoter and thus suppress its expression as well as invasiveness.
It has already been shown that small molecules can bind to the p53-binding site on the substrate binding site of mot-2 and release cytoplasmic p53 for nuclear localization, resulting in a p53-dependent apoptosis.
