We conclude that the presence of a CUX1 consensus binding site contributes to, but is not sufficient for, the recruitment of CUX1 to specific genomic locations.
These data suggest that the Sp1 binding site contributes to and the IRF-E plays an essential role in mediating the activity of the BAF complex.
However, while the narrow binding site contributes positively to the substrate selectivity, it negatively affects the affinity because of a decrease in entropy (see Appendix 1).
In addition to properly localizing focal adhesions and preserving RhoGAP activity, DLC1 interaction with tensin2 through this novel focal adhesion binding site contributes to the growth-suppressive activity of DLC1.
MOTIVATION: The DNA binding specificity of a transcription factor (TF) is typically represented using a position weight matrix model, which implicitly assumes that individual bases in a TF binding site contribute independently to the binding affinity, an assumption that does not always hold.
Motivation: The DNA binding specificity of a transcription factor (TF) is typically represented using a position weight matrix model, which implicitly assumes that individual bases in a TF binding site contribute independently to the binding affinity, an assumption that does not always hold.
This is supported by previous work showing that sets of non-binding positions coupled with a binding site contribute to the binding energy (Lockless and Ranganathan, 1999).
The PhyloP mammalian conservation track reports sequence conservation at the HNF4a binding site, contributing support to this site as a functional regulatory element.
However, PWM models make the assumption that individual bases in a TF binding site contribute independently and additively to the affinity of that site, which is not always true in practice.
Of the compounds studied, the compound 2FC4 showed high interaction with RT at non-nucleoside binding site, contributing high free binding energy (ΔG −8.01 Kcal) and IC50 (0.207 μg/ml), respectively.
