The GCN4 basic region-leucine zipper ( b/Zip ) binds DNA as a dimer of two uninterrupted a helices
Each monomer of GCN4 domain forms a smoothly curved continuous a helix. The monomers dimerized through zipper region. The basic regions bound to the DNA in the major groove on the opposite side.
GCN4 is a typical member of the b/Zip family of transcription factors. b/Zip family has more than 50 known members from yeast, mammalian and plant cells. GCN4 - 281 amino acids
- DNA-binding region in the C-terminal (~55 AA)
- basic region (~20 AA) -> 8 charged residues (Arg)
- zipper region (~35 AA) -> 4-3 repeat of Leu, Val
Homodimers bind to symetric DNA sequences Heterodimerization alter DNA-binding specificity
GCN4 binds to DNA with both specific and nonspecific contacts 4 amino acid side chain form sequence-specific contacts. Asn 235 is at the center of the interaction area
- strictly conserved in all b/Zip family members
- form 2 H-bondsMethyl side chains of Ala 238 and 239 form hydrophobic contacts with methyl group of T3 and T1, respectively.
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