Sentence examples for binding pocket may be from inspiring English sources

Based on these observations, we conclude that the generation of PXR antagonists targeted to the ligand binding pocket may be difficult due to the promiscuity and structural conformability of this xenobiotic sensor.

Instead, the general chemical, physical, and structural features of the binding pocket may be more important.

The enzyme exposes its active site through interfacial activation.[ 28] Crystal structures of CalA[ 29, 30] reveal a narrow acyl binding tunnel, a wider nucleophile binding cleft, and a flexible lid.[ 31] The wide nucleophile binding pocket may be the reason why CalA shows low enantioselectivity with small secondary alcohols.

Alternatively, the syntaxin 1A binding pockets may be similar in the KCNQ2 and KCNQ3 channels but differ in their interaction with other parts of the channels, which may interfere with the interaction of syntaxin 1A with helix A by preventing appropriate access to this site.

Current opinion suggests that classical competitive antagonists for PXR that bind in the ligand-binding pocket may be difficult to identify (Xue et al. 2007a) compared with allosteric antagonists that bind elsewhere on the protein surface (Ekins et al. 2007, 2008a).

Thus, binding site selection of cationic drugs in the QacR multidrug-binding pocket may be driven by a modulated, electrostatic tug-of-war that is in no small part driven by the formal negative charge carried by glutamate residues.

The complex of CYP3A4 with one substrate molecule bound in the substrate-binding pocket may be taken as a reasonable model of the catalytically competent complex.

This suggests that the majority of their substrate-binding pockets may be similar to each other.

Alternatively, the structural architecture of the cavity in the putative binding pocket may not be display.

Therefore, neither non-specific inhibition of MCL1 expression nor targeting the BH3-only binding pocket may ultimately prove to be clinically effective.

Nonetheless, our observations lead us to contend that a universal inhibitor for all APHs targeting the nucleotide-binding pocket may not be feasible, but the contrasting details between APH(3' -IIIa, APH(9)-Ia and ePKs suggests that selective inhibitors that target a subset of APHs is attainable.