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Molecular docking studies suggested that the dimers could bind simultaneously to the active site and the inhibitor binding pocket.
The orientation of inhibitor binding differs from natural folate binding.
A related measure of similarity that also uses inhibitor binding data is the correlations of inhibitor binding profiles between pairs of kinases.
This raises the question of how inhibitor binding is related to inhibitory affect.
A third measure of similarity is principle component analysis [85, 86] of multiple target-multiple inhibitor binding matrices (see "Methods").
Comparative docking studies were carried out to explore inhibitor binding characteristics within the X-ray structure and the model.
The two domains of sACE contain many conserved residues, which are vital for substrate and inhibitor binding (Table 4).
We used this docked model to postulate a mechanism for substrate transport and inhibitor binding for VAChT.
The influence of the replacement on the bioactivity and inhibitor binding was evaluated.
A detailed understanding of inhibitor binding therefore requires characterizing interactions across multiple activation states.
Upon inhibitor binding, the binding-site residues undergo subtle structural rearrangement.
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