Fig. 5.
Model of the dimer–dimer interface based on the NMR interactions, docking, and energy minimization. The key residues that interact in flp53, E171, V172, R174, and F212 are space-filled (C, gray; O, blue; N, red). The accessible surface area buried in the dimer interface in the modeled complex is 1,700 Å2, compared with 500 Å2 in the DNA-bound complex, with a gap volume index of 0.93. F212 interacts with V172 and F212 in the other subunit. E171 makes ionic interactions with R174 in the opposite subunit and R249 in its own subunit.