Figure 2.
Fig. 2. Sequences of the zinc finger peptides and of the
oligonucleotide binding sites. a, sequence of the wild type
Zif268 zinc finger peptide. The residues at positions 1, 2, 3,
and 6 of the helix of
finger one, which have been the focus of this study, are
circled. The three fingers are aligned to highlight conserved
residues and conserved secondary structure elements. The helix is
indicated by a cylinder, and the strands are
indicated by arrows. The cysteine and histidine residues that
are ligands for the zinc ions are highlighted in bold (adapted
from Ref. 12). b, sequences of the wild type and mutant
oligonucleotide binding sites used in the gel shift assays. The
Zif268 binding site is highlighted in bold; the numbering scheme
is the same as that used in papers describing the structure of
the complex (11, 12). Boxes indicate bases that are altered in
the mutant binding sites.
1, 2, 3,
and 6 of the 
helix of
finger one, which have been the focus of this study, are
circled. The three fingers are aligned to highlight conserved
residues and conserved secondary structure elements. The 
strands are
indicated by arrows. The cysteine and histidine residues that
are ligands for the zinc ions are highlighted in bold (adapted
from Ref. 12). b, sequences of the wild type and mutant
oligonucleotide binding sites used in the gel shift assays. The
Zif268 binding site is highlighted in bold; the numbering scheme
is the same as that used in papers describing the structure of
the complex (11, 12). Boxes indicate bases that are altered in
the mutant binding sites.