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Observation of the unfavorable energy impact of some residues (i.e. negatively charged E75 close to the binding site) could serve as valuable information for protein engineering aimed to improve the binding mode of GAGs to IL-8.
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Either visfatin or molecules that fit visfatin's binding site could help control the disease.
A metal bound to this site could serve to stabilize the RHH domains in a DNA-binding conformation, increasing the affinity of NikR for DNA.
Alternatively, this site could serve as a docking or phosphorylation site for a kinase that regulates binding of Fbxo15 to CLS1 indirectly.
Evaluations of selected articles on dedicated Internet sites could serve that purpose.
This fortuitous binding site could later prove to be a useful binding site for other low molecular mass partners.
Such interactions between elements around the binding sites could easily modulate affinity resulting in autoinhibition.
The cross-linked binding sites could be adsorbed to wheat germ agglutinin and to anion exchange resins.
Presumably, a ligand-binding site could exist in the groove.
The structure of survivin does not reveal hydrophobic binding pockets that could serve as docking sites for low molecular-weight ligands.
Of course in real TFs we expect that there will be a plateau for non-specific binding at some low affinity value [39], [40], but since we are only interested in the high affinity sites, which could serve as regulatory sites in vivo, we ignore that and consider the energies determined by the matrix to be the true binding energies for all potential binding sites.
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