The Cysteine-Rich Interdomain Region from the Highly Variable Plasmodium falciparum Erythrocyte Membrane Protein-1 Exhibits a Conserved Structure
Figure 8
MC179 forms a dimer in the crystal.
(A) Contact between the molecules is primarily between the helices (yellow) that connect the H2 and H3 helices and between the H1 (dark blue) to H3 (red) sides of the three-helix bundles. (B) The molecular surface of the crystalline dimer shows the intertwining of the two molecules in a “handshake” manner. One molecule (at right) is colored by sequence conservation in a ramp of blue to white as in Figure 3, and the other molecule (at left) is colored gray for contrast. The total buried solvent-accessible surface area is 4300 Å2. The surface complementarity is 0.70 [46] and 55 residues (220 atoms) from each molecule take part in the interaction. The two MC179 molecules are related by a crystallographic two-fold symmetry axis. The locations of several residues are indicated.