Figure 1.

Structural organization of the dimer interface in 14-3-3ζ. A, schematic representation of the predicted salt bridges at the dimer interface of 14-3-3ζ. The orange and green modules represent two monomer units of 14-3-3ζ, and residues shown in large boldface type represent predicted salt-bridging residues conserved across multiple 14-3-3 isoforms. The buried Ser⁵⁸ phosphorylation site is also shown in pink. B, the dimer interface of 14-3-3ζ (residues 1–110) is shown in a ribbon representation with predicted key salt-bridging residues highlighted (acidic residues in yellow and basic residues in blue). The buried Ser⁵⁸ phosphorylation site is shown in pink. The inset shows the dimer interface in greater detail with the predicted salt bridge residues labeled. C, an alignment of the N-terminal primary sequences encompassing the dimer interface of all seven isoforms of human 14-3-3 ζ, β, η, γ, ϵ, τ, and σ, with the predicted salt bridge residues highlighted and their proposed intermolecular interactions represented by dotted lines. The positions of the first four α-helices are indicated as αA, αB, αC, and αD.