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Exact(18)
The co-crystal structure proves that compound 3 binds in the same orientation as PLP, and confirms the mode of inhibition to be competitive.
The Blm10 C terminus binds in the same manner as seen for 11S activators and inferred for 19S/PAN activators and indicates a unified model for gate opening.
Regarding compound 3s, the 2D and 3D ligand interaction simulations (Figs. 4 and 5) showed that 3s binds in the same fashion to the co-crystallized ligand displaying two hydrogen bonds with the active pocket amino acid Met 98 leading to an overall binding energy of = −11.64 kcal/mol (Table 3).
This is in agreement with the structural observation that ring I binds in the same orientation irrespective of the substituents at the 2-deoxystreptamine ring [18].
Cryoelectron microscopy followed by image reconstruction of HS-adapted RRV revealed that HS binds in the same outermost region of the E2 glycoprotein as MAb T10C9 [56].
The template-primer also binds in the same register as in the undamaged complex, and there is little or no movement of the N-clasp in accommodating an 8-oxoG adducted DNA.
Similar(41)
The docking study was performed using the LigandFit option of receptor ligand interactions protocol section available in Discovery Studio 2.1 where lower RMSD values (0.6931 Å) between the co-crystallized ligand and re-docked ligand assured that the ligand was bound in the same binding pocket.
At around the same time, a series of isoxazolidine-containing molecules named iTADs were described that bind in the same binding site of KIX as transactivation domains of proteins such as MLL, c-Jun, and Tat.
The observation that double combinations of neuraminidase inhibitors were not synergistic is consistent with the fact that all three drugs are known to target the same enzyme, and all bind in the same substrate binding pocket in a similar manner [19].
In general, fingerprint scoring yielded especially good results when the ligands in known complex structures bind in the same regions of the binding site, exhibit similar interactions and show a high affinity.
All three ligands bound in the same pocket of CRBN and demonstrated similar binding modes, and very tight interaction with KD values of 250 nM (thalidomide), 178 nM (lenalidomide) and 157 nM (pomalidomide) measured by FP assays.
More suggestions(15)
interconnects in the same
ties in the same
extends in the same
binding in the same
binds in the central
binds in the DFG-out
binds in the present
binds in the vWC1
binds in the minor
binds in the major
binds in the flipped
binds in the fatty
binds in the substrate-binding
binds in the second
binds in the hydrophobic
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