These potential binding sites, which are now recognized as Molecular Recognition Features (MoRFs), occur as dips on the plot of disorder score, and correspond to segments with an increased propensity towards order that are flanked by disordered regions.
Animal miRNAs recognize partially complementary binding sites, which are generally located in the 3′ untranslated region (3′UTR) of target mRNAs.
The sequence of this binding site does not resemble any known ATP binding sites, which have much higher binding affinities.
Overall, these results show that D44 and E116 residues are important for the catalytic activity of Cj-RNase III by providing a metal-binding site, which is recognized by Mg2+ and Mn2+.
Any binding site which had a p < 0.01 was annotated as a potential miRNA binding site.
Many of those located within the cytoplasmic tail of the receptor create binding sites for proteins containing Src homology 2 (SH2) and phosphotyrosine-binding (PTB) domains, which recognize phospho-Tyr residues within the context of specific adjacent amino acids.
Phosphorylation of protein substrates creates binding sites for protein domains which recognize specific phosphorylated amino acid sequences, thereby mediating protein-protein interactions [3], [4].
Unlike bisulfite sequencing, MIRA and MeDIP simulate the in vivo behavior of methyl-CpG binding domain (MBD) proteins, which recognize both the methylation level and concentration of individual CpG sites [ 38].
NtcA is a promoter binding protein (PBP), which recognizes a conserved sequence within the chivosazol promoter.
The regulation of gene expression in a cell relies to a major extent on transcription factors, proteins which recognize and bind the DNA at specific binding sites (response elements) within promoter regions associated with each gene.
