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The Basic Leucine Zipper Domain (bZIP domain) is found in many DNA binding eukaryotic proteins. One part of the domain contains a region that mediates sequence specific DNA binding properties and the leucine zipper that is required to hold together (dimerize) two DNA binding regions.
The bZIP domain is 60 to 80 amino acids in length with a highly conserved DNA binding basic region and a more diversified leucine zipper dimerization region. [4] The localization of the leucines are critical for the DNA binding to the proteins.
AP-1 was first discovered as a TPA-activated transcription factor that bound to a cis-regulatory element of the human metallothionein IIa promoter and SV40. [3] The AP-1 binding site was identified as the 12-O-Tetradecanoylphorbol-13-acetate response element (TRE) with the consensus sequence 5’-TGA G/C TCA-3’. [4]
bZIP Maf is a domain found in Maf transcription factor proteins. It contains a leucine zipper (bZIP) domain, which mediates the transcription factor's dimerization and DNA binding properties. The Maf extended homology region (EHR) is present at the N-terminus of the protein.
NRF2 possesses seven highly conserved domains called NRF2-ECH homology (Neh) domains. The Neh1 domain is a CNC-bZIP domain that allows Nrf2 to heterodimerize with small Maf proteins (MAFF, MAFG, MAFK). [12] The Neh2 domain allows for binding of NRF2 to its cytosolic repressor Keap1. [13]
A DNA-binding domain (DBD) is an independently folded protein domain that contains at least one structural motif that recognizes double- or single-stranded DNA.A DBD can recognize a specific DNA sequence (a recognition sequence) or have a general affinity to DNA. [1]
MafF has a bZIP structure that consists of a basic region for DNA binding and a leucine zipper structure for dimer formation. [5] Similar to other sMafs, MafF lacks any canonical transcriptional activation domains.
DNA-binding proteins are proteins that have DNA-binding domains and thus have a specific or general affinity for single- or double-stranded DNA. [ 3 ] [ 4 ] [ 5 ] Sequence-specific DNA-binding proteins generally interact with the major groove of B-DNA , because it exposes more functional groups that identify a base pair .