The AC family of proteins binds both globular (G-Actin) and filamentous actin (F-actin) and this binding is regulated by multiple mechanisms: phosphorylation, interaction with polyphosphoinositides, pH, and competitive binding interactions with other actin binding proteins [13], [14].
Furthermore, the binding kinetics of 15 mutants revealed that binding is regulated by long-range interactions, which can be correlated with the structural rearrangements resulting from peptide binding.
Vector release or binding is regulated by the effective affinity of the vector for the polymer, which depends upon the strength of molecular interactions.
Transcription factor binding is regulated by several interactions, primarily involving cis-element binding.
The specificity of aldosterone-MR binding is regulated by cortisol levels and 11 β-HSD2 enzyme expression.
TF-promoter binding is regulated by nucleosomes, segments of DNA wrapped around histone proteins that are the fundamental repeating unit of chromatin structure, that restrict access to potential operator sites.
Identified conserved binding sites were regulated by 73 transcription factors, including CREB, HNF1, NRF2, FOXP3, and factors from Pax, Gata and Stat families.
S6 segments are also involved in drug binding, and this binding can be regulated by β subunits [15], [39].
DNA binding may be regulated by sequences bordering the Ets; for instance, ETS1 DNA binding is inhibited by two helices flanking each side of the Ets.
The function of p53 and its promoter binding capacity is regulated by a number of posttranslational modifications but also by various cofactors [46], [47] and is therefore largely dependent on the cellular context.
