Expanded view of the interaction of Nb67 with the two sides of the Cap domain. The interaction with Nb67 A (Left) shows no distortion of the helices, whereas interaction with N67 B on the opposite side results in unwinding of EH1 B (residues E113, E116 and D120 are unique in TREK-2 vs TREK-1). Right: the interaction of N108 with NB67 B differs on the side where EH1 B is unwound. This interaction does not occur with Nb67 A .
