Figure 1.
FIGURE 1. The TREX1 dimer in complex with ssDNA. The TREX1
exonuclease dimerizes about a 2-fold axis perpendicular to the
-strands (monomers shown
in blue and green). This interaction creates an extended
anti-parallel -sheet through the core
of the dimer and places the two active sites on opposite outer
edges. The complex contains ssDNA (shown as sticks) and Ca^2+
(shown as red spheres) bound in both of the active sites.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2007,
282,
10537-10543)
copyright 2007.
-strands (monomers shown
in blue and green). This interaction creates an extended
anti-parallel