The DNA-binding domain (DBD) of the Estrogen Receptor (ER) features zinc fingers that significantly influence the receptor’s ability to interact with Estrogen Response Elements (EREs).
Within the first zinc finger is a region termed the proximal box (P-Box), where three specific amino acids are crucial for sequence-specific binding to the ERE. However, it remains uncertain which nucleotides in the ERE bind with these P-Box amino acids with the highest affinity, as different experimental techniques result in inconsistent findings.
The second zinc finger of the Estrogen Receptor (ER) serves two primary functions:
Dimerization: It facilitates the dimerization of ER, a necessary step for DNA binding and initiating transcriptional activation.
ERE Half-Site Spacing Recognition: It discerns the spacing between half-sites in an ERE, ensuring accurate ER alignment with the DNA sequence.
