Sentence examples for binding pocket due to from inspiring English sources
Importantly, the centroid of each peptide does not form interactions with binding pocket due to displacement by abacavir.
Arg101 lies further away from the substrate binding pocket due to the different conformation of this loop in both structures (Fig. 3a).
Furthermore, M311 was assigned a variety of roles in the past including tentative participation in stabilization of Tl+ in the binding pocket due to high polarizability.
In the three other simulations, deacetylated Lys23 remained localized to the binding pocket due to electrostatic interactions with Glu30 (refer to Figure 6A for positions of residues).
The P2Y12R– 34 antagonist complex structure (PDB ID 4NTJ) revealed a wide open binding pocket due to the unresolved ECL1 and ECL2 regions and the outward positions of helices VI (TM6) and VII (TM7).
Our original crystal structure of rMUP in the absence of ligand[ 10] (PDB ID: 1QY0) was not suitable for the observation of ordered solvent water molecules within the binding pocket due to the presence of cryoprotectant glycerol.
The homology models of the α4β2 and α3β4 nicotinic acetylcholine receptors (nAChRs) suggest that the two nAChR subtypes are different in their ligand-binding pockets due to the non-conserved residues in the β-subunits.
Further, studies have suggested that the sugar donor and acceptors are accommodated in the cavity between the N and C terminal domain and the formation of substrate binding pocket is due to several regions in the primary sequence of the protein [ 41].
Previous investigations identified an α4−α4 binding site and suggested the differences between the "high" affinity (α4−β2) and "low" affinity (α4−α4) binding pockets are due to three key residues that reside on the complementary face.
Overall, these results support the findings of An et al. (2005) that ligand binding pockets are almost always retained in unbound structures and furthermore that the prediction accuracy is not significantly degraded by differences in these pockets due to structural changes upon ligand binding.
As such, it was recently proposed that subtle differences in the size of the arginine-binding pocket, mainly due to alterations of the THW loop, may be important for controlling the product selectivity of the PRMTs.
