Our results point to the importance of incorporating dynamic information when predicting functional sites. Furthermore, our analysis of the catabolite activator protein, which is allosteric without conformational change, shows that its regulation involves other types of motion than those modulated at sites with high binding leverage. For the majority of the analyzed proteins, we find that both catalytic and allosteric sites have high binding leverage. We analyze single catalytic domains and multimeric allosteric enzymes with complex regulation. We use Monte Carlo simulations to generate potential binding sites and either normal modes or pairs of crystal structures to describe relevant motions. We introduce a quantity called binding leverage that measures the ability of a binding site to couple to the intrinsic motions of a protein. ![]() ![]() Allosteric regulation involves conformational transitions or fluctuations between a few closely related states, caused by the binding of effector molecules.
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