Figure 3. Stereo image showing the conformation of the four
H2 helices in a ZapA tetramer with their side-chains exposed.
The tetramerisation domain is formed by extensive overlap
between the C termini of the H2 helices. This region is
characterised by a central hydrophobic core and surrounding
hydrophilic amino acid residues with interdigitating
side-chains. In contrast, the dimerisation domain is located
towards the opposite ends of the H2 helices with inter-helix
proximity and contact increasing towards the N termini.
The above figure is reprinted
by permission from Elsevier:
J Mol Biol