In the present study, the DNA-binding domain recognized by three RelBE-like pairs and its structural characteristics were revealed.
The physical interactions between the three pairs of RelBE proteins were confirmed and the DNA-binding domain recognized by three RelBE-like pairs and domain structure characteristics were described.
In Table 6, DNA-binding domains recognized by Pfam [ 46] will be classified into five binding modes, including zipper-type, helix-turn-helix (HTH), zinc-coordinating, β-hairpin/ribbon, and others.
Apparently, inhibition of DKK1 binding to LPR6 within the E1 domain, recognized by this antibody, or the E3-E4 domain, bound by YW211.31 antibody, contributes only weakly to the antagonism of DKK1 activity by these antibodies.
We used a two-step strategy: Firstly, by a competition binding assay, we identified the proper boundaries of the domain recognized by 2F5, which we found considerably larger than the ELDKWAS hexapeptide.
Similarly, Bromo domains recognize acetylation sites and Ubiquitin binding domains recognize ubiquitin.
The N-terminus MH1 domain is a DNA-binding domain recognizing CAGA motifs.
By combining secondary structure predictions and protein sequence alignments, we predicted the DDE catalytic triad and the DNA-binding domain recognizing the terminal inverted repeats.
We previously showed that two separate regions in fibronectin, the N-terminal and the adjoining gelatin-binding domains, are recognized by recombinant Lig proteins comprising the variable immunoglobulin-like repeats (C-terminal half of LigA, repeats 7' to 13, and the middle portion of LigB, repeats 7' to 12; the proteins LigA U and LigB U1, respectively [15]).
However, variability in the DNA binding sequences recognized by TF binding domains may complicate the results.
