|
Figure 3.
Figure 3. Protein-DNA and protein-protein interactions at
the dimer interfaces. (a) Close-up view of the protein-protein
contacts in the DR1 complex formed by subunits 1 and 2, and
equivalently by subunits 3 and 4. The pink bars indicate the
position of the spacer base-pair(s). Side-chains shown are only
those making DNA or dimerization contacts. Hydrogen bonding
between the side-chains of residues 49, 52 and 74, which form
the dimerization contacts, are shown by broken lines. Figures
were generated with Ribbons [Carson and Bugg 1986]. (b) The
corresponding view at the "DR2" site. (c) Surface
complementarity in the protein-protein interface on DR1, with
subunit 1 shown in red and subunit 2 shown in white. The
location of the DNA is shown for reference, with the 5' end
pointing up [Nicholls et al 1991]. (d) The corresponding view at
the "DR2" interface, with subunit 2 (white) and subunit 3
(blue). (e) Fluorescence anisotropy measurements showing the
binding of RXR-DBD to DR1 (black circles) and DR2 (red squares).
The maximal values for fluorescence aniostropy differ for the
DR1 and DR2 plots, as expected from the different binding
geometries and solution reorientation properties of these
complexes.
|
