Electrostatic surface potential of the HMG-1 box
The surface potential of the second HMG-1 box from rat HMG-1
is shown below. The
majority of negatively-charged surfaces (shown in red) are
located towards the bottom of the model, while there are several
basic surfaces (shown in blue) on the opposing, concave surface.
The conserved, positively-charged lysine and arginine residues
flanked by prolines at positions 2 and 3 may be responsible for
anchoring the DNA onto the concave surface of the protein. In
addition, it has been proposed for human SRY that Ile 9
interacts with DNA through partial sidechain intercalation in
the minor groove
(King & Weiss, 1993).
Side view
Top view