2L5Y
NMR structure of calcium-loaded STIM2 EF-SAM.
Summary for 2L5Y
| Entry DOI | 10.2210/pdb2l5y/pdb |
| NMR Information | BMRB: 17289 |
| Descriptor | Stromal interaction molecule 2, CALCIUM ION (2 entities in total) |
| Functional Keywords | stromal interaction molecule, ef-hand, sam domain, store operated calcium entry, signaling protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 17871.05 |
| Authors | Zheng, L.,Stathopulos, P.B.,Ikura, M. (deposition date: 2010-11-09, release date: 2011-01-19, Last modification date: 2024-05-01) |
| Primary citation | Zheng, L.,Stathopulos, P.B.,Schindl, R.,Li, G.Y.,Romanin, C.,Ikura, M. Auto-inhibitory role of the EF-SAM domain of STIM proteins in store-operated calcium entry. Proc.Natl.Acad.Sci.USA, 108:1337-1342, 2011 Cited by PubMed Abstract: Stromal interaction molecules (STIM)s function as endoplasmic reticulum calcium (Ca(2+)) sensors that differentially regulate plasma membrane Ca(2+) release activated Ca(2+) channels in various cells. To probe the structural basis for the functional differences between STIM1 and STIM2 we engineered a series of EF-hand and sterile α motif (SAM) domain (EF-SAM) chimeras, demonstrating that the STIM1 Ca(2+)-binding EF-hand and the STIM2 SAM domain are major contributors to the autoinhibition of oligomerization in each respective isoform. Our nuclear magnetic resonance (NMR) derived STIM2 EF-SAM structure provides a rationale for an augmented stability, which involves a 54° pivot in the EF-hand:SAM domain orientation permissible by an expanded nonpolar cleft, ionic interactions, and an enhanced hydrophobic SAM core, unique to STIM2. Live cells expressing "super-unstable" or "super-stable" STIM1/STIM2 EF-SAM chimeras in the full-length context show a remarkable correlation with the in vitro data. Together, our data suggest that divergent Ca(2+)- and SAM-dependent stabilization of the EF-SAM fold contributes to the disparate regulation of store-operated Ca(2+) entry by STIM1 and STIM2. PubMed: 21217057DOI: 10.1073/pnas.1015125108 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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