Sentence examples for binding pocket in a from inspiring English sources

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].

The NCIDS enabled us to test more extensively the conformational space of the ligands inside the binding pocket in a reasonable amount of time.

Consequently, these MM models show that molecular oxygen does not fit into the binding pocket in a position trans to His187 as it is too tight with too many closely packed residues.

In contrast, the heterocyclic part of 6 was relatively planar and slotted into the ATP binding pocket in a manner typical for type I ATP-competitive kinase inhibitors: it formed a key hydrogen bond between the backbone amide of Val96 in the kinase hinge region and N-7 of the imidazo-pyramidazine portion of the ligand.

To determine if an indolocarbazole-like substrate could enter the binding pocket in a reduced-RebC state, the program CAVER was used (22) to identify the favored path by which a probe placed in the active site would escape to the solvent.

The term 'atypical' is used for an amino acid that has not been observed in a particular binding pocket in any known substrate for a peptidase.

The docking-based alignment succeeded in accessing self-consistent CoMFA models upon employing JAIN scoring function in one of the proposed binding pockets in a particular homology model.

Together, the comparison of DRCs for purine-like leads suggests that 5– 8 may bind the ATP-binding pocket in a different orientation than adenine and that the enzymes are highly discerning about what moieties can be added at this position as a large number of related molecules did not inhibit multiple HKs (Supporting Information Table 1, compounds S4, S27 38).

We have used spin-labeled ADP to investigate the dynamics of the nucleotide-binding pocket in a series of myosins, which have a range of velocities.

In particular, the R325 side chain interacts with both the 3′OH and the 4′PO42− of the PIP2 molecule; the stability of the interaction between the ζ-carbon of the Kv7.2 residuesidue and the phosphorus atom at C4′ of PIP2 was confirmed by molecular dynamics experiments over a 10 ns time range (Suppl. Fig. 1). Figure 4: Location of the R325 residue within a PIP2-binding pocket in a Kv7.2 subunit.

In addition, they interact with the colchicine-binding pocket in a unique manner: our docking studies suggest that the R-isomers interact with tubulin via their furan ring, while the S-isomers localize to the colchicine pocket via their ester side chain.