Harris et al. Figure 3
Computer models of the ER DBD from X-ray crystallographic structure
determination (PDB structure ID:
1HCQ) docked at a 25bp DNA sequence from
Genebank locus XLVIT15 (see figure 2c). Amino acid and codon alignments are highlighted on the protein and DNA
respectively. All highlighted residues have a dot surface indicating the van der Waals surfaces of each
atom in that residue. The DNA nucleotides are color
coded: Ade = green, Thy = red, Gua = yellow and Cyt = blue. Color coding of amino acids is based on
polarity: positively charged side chains = blue, negatively charged side chains = red,
uncharged polar side chains = yellow and nonpolar side chains = purple. The protein is docked at a
distance of about 10 angstroms from the DNA for visual clarity.
a. Lysine residues from the exon 2 encoded DNA recognition helix (K206 and K210)
and lysine codons in the DNA are highlighted. Amino acids are numbered as in
human ER (37).
b. Exon 2 encoded DNA recognition helix phenylalanine (F208) residues and phenylalanine
codons are highlighted.
c. Serine residues from the exon 2 encoded DNA recognition helix (S212) and serine codons are
d. Glutamine residues from the exon 2 encoded DNA recognition helix (Q214)
and exon 3 encoded beta strand (Q238) and glutamine codons are highlighted.
e. Exon 3 encoded beta strand histidine residues (H216) and histidine codons are highlighted.
f. Exon 3 encoded beta strand aspartic acid residues (D218) and aspartic acid codons are highlighted.