Sentence examples for binding pocket as a from inspiring English sources

To investigate this possibility, we have engineered the pig OBP, whose three-dimensional structure has been resolved, introducing a tryptophan residue in the core of the binding pocket, as a fluorescence reporter for the presence of bound ligands.

A mechanism-based, peptide-derived inhibitor indeed showed an IC50 of 4 μM for Sirt1, and ~17-fold and >77-fold lower potency against Sirt2 and Sirt3, respectively [ 35], indicating the peptide binding pocket as a promising target site.

While these analogues might suggest a limited tolerance for further elaboration of the aryl ring, modifications at corresponding positions of other kinase scaffolds has enabled access to an additional hydrophobic binding pocket as a result of a switch to the DFG-out conformation.

Specifically, we analyzed the role of the putative proton-coupling motif 41ExxER45; the role of charged residues in the extended loop R264R266K267; and residues in the substrate binding pocket as well as a predicted a salt bridge L49, K164, Q358, Y388, and E476 (Newstead, 2011; Newstead et al., 2011; Solcan et al., 2012; Doki et al., 2013).

Supporting NMR titration data further indicated that this peptide binds with the phosphothreonine in the canonical binding pocket as might be predicted.

However, it enables in some instances the simultaneous binding of two or even three molecules, which interact with the binding pocket as well as with each other, resulting in a more stable binding conformation [199].

Moreover, several residues known to be critical in the caspase-3 catalytic centre and binding pocket, as well as the active-site pentapeptide motif Q172ACRG176 were present in the deduced Lyccasp3.

This observation proves that the helix orientation of TM2 can change and modulate the size and shape of the binding pocket, as well as form direct/indirect interactions with the substituents attached to the 6-position of the central pyrimidine (we discuss this point further in Supplementary Note 1).

Accordingly, the orientation of the retinal in its binding pocket, as known from the dark state rhodopsin structure[1], determines its longitudinal orientation during uptake and release.

The co-crystal structure of PAP and TBBPA bound to SULT1E1 reveals TBBPA binding in the same substrate binding pocket as E2.

These functional sites include the residues involved in coordinating Na+ and GABA in the transporter binding pocket, as well as those that serve as extracellular and cytoplasmic gates.