Fig. 8
From: A dual mechanism promotes switching of the Stormorken STIM1 R304W mutant into the activated state
Hypothetical conformational models of STIM1 wt and STIM1 R304W in resting cell conditions. STIM1 domains (top). STIM1 wt (left) packs into a tight conformation as a result of the intramolecular CC1–CC3 clamp interaction. STIM1 R304W (right), in contrast, assumes an extended conformation. The STIM1 R304W mutation (i) increases CC1α2 helicity and stiffens the linker region between CC1α2 and CC1α3, which together with (ii) an enforced CC1–CC1 homomerization antagonizes formation of the CC1–CC3 clamp
