Crystal structure of Nb-binder-58 (Nb58) in complex with TREK-2. This functionally inactive tight binder interacts as a dimer with the tip of the Cap domain only. The relative position of the C terminus of each Nb58 chain is indicated. The right-hand panel shows an expanded view of the interactions involved and shows the C123 disulphide between chains at the apex of the Cap. D120 and V122 are unique in TREK-2 compared to other TREK channels.
