Sentence examples for binding pocket of both from inspiring English sources

Given that identical residues line the DMXAA binding pocket of both mSTING and hSTING, it is unclear why DMXAA only activates mSTING.

We have compared the genome-wide effects on the transcriptome after treatment with ICG-001 (the specific CBP inhibitor) versus C646, a compound that competes with acetyl-coA for the Lys-coA binding pocket of both CBP and p300.

We have compared the genome-wide effects on the transcriptome of ICG-001 (a specific CBP inhibitor) versus C646 (a compound that competes with acetyl-coA for the Lys-coA binding pocket of both CBP and p300).

In our study, we compare the effects of treatment with C646, which is thought to compete with acetyl-coA for the Lys-coA binding pocket of both p300 and CBP [ 11] to the effects of ICG-001, which specifically binds to CBP and prevents its interaction with the co-activator β-catenin.

Additionally, structural interaction fingerprints analysis identified the important amino acid residues for the specific interactions of long-chain arylpiperazines within the binding pockets of both serotonin receptors.

To understand the species selectivity in a series of α-methyl-α-phenoxy carboxylic acid PPARα/γ dual agonists (1 11), structure-based molecular modeling was carried out in the ligand binding pockets of both human and mouse PPARα.

The fused bifunctional enzyme therefore represents an excellent vehicle for finding inhibitors that engage the pterin binding pockets of both modules that have entirely different architectures.

The fluorenyl moiety is sandwiched between the hydrophobic groups of residues Lys15, Lys15', Leu17, Leu17', Thr106, Thr106', Ala108, Ala108', Val121 and Val121' in the outer binding pockets of both AC and BD dimer.

On the basis of the results obtained in docking simulations as described in the Materials and methods section, we evaluated the affinity of MIBE for the ligand binding pockets of both ERα and GPER with respect to E2 and G-1, respectively.

The main difference in the acyl-binding pocket of both these enzymes is that F288 and F290 in AChE were replaced by L286 and V288 of BChE [ 17].

Although bending toward the binding pocket of the receptor, both the N- and C-terminal ends of the EL2 loop protrude across the interface toward the other protomer (see Figure 4), hindering tighter packing between the helices deeper in the membrane and at the intracellular ends of the protomers.