  14-3-3 proteins are a group of seven dimeric adapter proteins that exert
their biological function by interacting with hundreds of phosphorylated
proteins, thus influencing their sub-cellular localization, activity or
stability in the cell. Due to this remarkable interaction network, 14-3-3
proteins have been associated with several pathologies and the protein-protein
interactions established with a number of partners are now considered promising
drug targets. The activity of 14-3-3 proteins is often isoform specific and to
our knowledge only one out of seven isoforms, 14-3-3$\zeta$, has been assigned.
Despite the availability of the crystal structures of all seven isoforms of
14-3-3, the additional NMR assignments of 14-3-3 proteins are important for
both biological mechanism studies and chemical biology approaches. Herein, we
present a robust backbone assignment of 14-3-3$\sigma$, which will allow
advances in the discovery of potential therapeutic compounds. This assignment
is now being applied to the discovery of both inhibitors and stabilizers of
14-3-3 protein-protein interactions.
