6YEL
Stromal interaction molecule 1 coiled-coil 1 fragment
Summary for 6YEL
| Entry DOI | 10.2210/pdb6yel/pdb |
| NMR Information | BMRB: 50114 |
| Descriptor | Stromal interaction molecule 1 (1 entity in total) |
| Functional Keywords | calcium signaling, store-operated ca2+ entry, crac, signaling protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 13922.58 |
| Authors | Rathner, P.,Cerofolini, L.,Ravera, E.,Bechmann, M.,Grabmayr, H.,Fahrner, M.,Fragai, M.,Romanin, C.,Luchinat, C.,Mueller, N. (deposition date: 2020-03-25, release date: 2020-09-02, Last modification date: 2024-06-19) |
| Primary citation | Rathner, P.,Fahrner, M.,Cerofolini, L.,Grabmayr, H.,Horvath, F.,Krobath, H.,Gupta, A.,Ravera, E.,Fragai, M.,Bechmann, M.,Renger, T.,Luchinat, C.,Romanin, C.,Muller, N. Interhelical interactions within the STIM1 CC1 domain modulate CRAC channel activation. Nat.Chem.Biol., 17:196-204, 2021 Cited by PubMed Abstract: The calcium release activated calcium channel is activated by the endoplasmic reticulum-resident calcium sensor protein STIM1. On activation, STIM1 C terminus changes from an inactive, tight to an active, extended conformation. A coiled-coil clamp involving the CC1 and CC3 domains is essential in controlling STIM1 activation, with CC1 as the key entity. The nuclear magnetic resonance-derived solution structure of the CC1 domain represents a three-helix bundle stabilized by interhelical contacts, which are absent in the Stormorken disease-related STIM1 R304W mutant. Two interhelical sites between the CC1α and CC1α helices are key in controlling STIM1 activation, affecting the balance between tight and extended conformations. Nuclear magnetic resonance-directed mutations within these interhelical interactions restore the physiological, store-dependent activation behavior of the gain-of-function STIM1 R304W mutant. This study reveals the functional impact of interhelical interactions within the CC1 domain for modifying the CC1-CC3 clamp strength to control the activation of STIM1. PubMed: 33106661DOI: 10.1038/s41589-020-00672-8 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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