Fig. 5
From: Focused clamping of a single neuronal SNARE complex by complexin under high mechanical tension
Multiple domains of complexin collectively drives SNARE complexes into the linker-open conformation. a The domain structures of wild-type Cpx and its variants prepared in this study. b Force–extension curves for unzipping (blue/black) and rezipping (gray) of SNARE complexes in the presence of the indicated variants of Cpx (all at 5 μM). Horizontal scale bar represents 20 nm. c Force-dependent evolution of extensions for the SNARE complex between 13 and 16 pN of force in the presence of the indicated variants of Cpx. d Force-dependent equilibria among the three zippered conformations. Solid lines represent the fits to a three-state equilibrium model (Supplementary Note 5). The curves for wild-type Cpx (WT) are overlaid as shades in the top panel with NAC for the sake of comparison. The color code is the same as in c. e, f Fold changes at 14 pN in the half-zippered (e) and linker-open (f) populations upon addition of each Cpx variant. In d–f, data are represented as mean ± s.d. of more than three measurements. g, h Representative time traces for the SNARE complexes in the presence of the indicated variants of Cpx. Vertical and horizontal scale bars represent 10 nm and 50 ms, respectively
