Resonance assignment of coiled-coil 3 (CC3) domain of human STIM1

The protein stromal interaction molecule 1 (STIM1) plays a pivotal role in mediating store-operated calcium entry (SOCE) into cells, which is essential for adaptive immunity. It acts as a calcium sensor in the endoplasmic reticulum (ER) and extends into the cytosol, where it changes from an inactive (tight) to an active (extended) oligomeric form upon calcium store depletion. NMR studies of this protein are challenging due to its membrane-spanning and aggregation properties. Therefore follow the divide-and-conquer approach, focusing on individual domains first is in order. The cytosolic part is predicted to have a large content of coiled-coil (CC) structure. We report the H-1, C-13, N-15 chemical shift assignments of the CC3 domain. This domain is crucial for the stabilisation of the tight quiescent form of STIM1 as well as for activating the ORAI calcium channel by direct contact, in the extended active form.

Automated summary

The protein STIM1 is crucial for store-operated calcium entry and changes from an inactive to an active form in response to calcium depletion. Studies of STIM1's CC3 domain are important for understanding its role in stabilizing the inactive form and activating the ORAI calcium channel.