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14-3-3 proteins are a group of seven dimeric adapter proteins that exerttheir biological function by interacting with hundreds of phosphorylatedproteins, thus influencing their sub-cellular localization, activity orstability in the cell. Due to this remarkable interaction network, 14-3-3proteins have been associated with several pathologies and the protein-proteininteractions established with a number of partners are now considered promisingdrug targets. The activity of 14-3-3 proteins is often isoform specific and toour 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 of14-3-3, the additional NMR assignments of 14-3-3 proteins are important forboth biological mechanism studies and chemical biology approaches. Herein, wepresent a robust backbone assignment of 14-3-3$\sigma$, which will allowadvances in the discovery of potential therapeutic compounds. This assignmentis now being applied to the discovery of both inhibitors and stabilizers of14-3-3 protein-protein interactions.

Backbone chemical shift assignments of human 14-3-3$\sigma$