Harris et al. Figure 1
Computer models of the GR DBD from NMR structure determination with putative flanking alpha helices attached docked at a 29bp DNA sequence of Genebank locus MMTPRGR1. 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 3 encoded DNA recognition helix (K461 and K465) and exon 5 encoded predicted alpha helix (K511, K513, K514, K515 and
K517) in the protein and lysine codons in the DNA are highlighted.
B. Exon 3 encoded DNA recognition helix valine (V462) residues and valine codons are highlighted.
C. Arginine residues from the exon 3 encoded DNA recognition helix (R466) and exon 5 encoded predicted alpha helix (R 510) and arginine codons are highlighted.
D. Exon 3 encoded DNA recognition helix glutamic acid (E469) residues and glutamic acid codons are highlighted.
E. Exon 4 encoded beta strand glutamine residues (Q471) and glutamine codons are highlighted.
F. Exon 4 encoded beta strand asparagine residues (N473) and asparagine codons are highlighted.
G.Exon 4 encoded beta strand tyrosine residues (Y474) and tyrosine codons are highlighted.
H. Exon 4 encoded leucine residues (L475) of the beta strand and (L507) located in the carboxyl region of the GR DBD and leucine codons are highlighted.