Structural features of the 14-3-3γ. (A) The 14-3-3 proteins con-sist of nine α--helical bundles to form a dimer for making a U-shaped groove. The first and second helices of the N-terminus of one monomer are connected to the fourth helix of the other monomer by the salt bridge. The first, third, fifth and seventh helices of one monomer are located inside the cup, and the third, fifth, seventh and ninth helices form a conserved amphiphilic groove that binds to the target protein. (B) The 14-3-3γ is a highly conserved protein that has the same protein sequence in humans, rat, and mice. Like most isotypes, the 14-3-3γ consists of nine helical structures.