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TitleStructural dynamics of the human Orai1 channel revealed by cryo-electron microscopy.
Journal, issue, pagesPLoS One, Vol. 21, Issue 5, Page e0348440, Year 2026
Publish dateMay 11, 2026
AuthorsYiming Zhang / Yuan Wang / Jindou Liu / Weiwei Bei / Hongkun Wang / Junli Wang / Lei Chen / Youjun Wang /
PubMed AbstractThe pore-forming Orai1 protein is an essential component of store-operated calcium entry (SOCE), a process vital to diverse cellular and physiological functions. Mutations in human Orai1 cause severe ...The pore-forming Orai1 protein is an essential component of store-operated calcium entry (SOCE), a process vital to diverse cellular and physiological functions. Mutations in human Orai1 cause severe immunodeficiencies and myopathies, yet structural insights have remained largely elusive. To address this, we studied the structure of detergent-solubilized human Orai1 (hOrai1) by cryo-electron microscopy. While the overall resolution is moderate, the reconstructed map confirms a conserved hexameric architecture and enables assignment of transmembrane helices. We observed profound structural heterogeneity, with particles adopting both C6- and C2-symmetric conformations, indicative of dynamic rearrangements. This study establishes a framework for future structural and mechanistic studies of hOrai1.
External linksPLoS One / PubMed:42113836 / PubMed Central
MethodsEM (single particle)
Resolution4.52 - 4.97 Å
Structure data

EMDB-66969: human ORAI1 in C6 symmetry
Method: EM (single particle) / Resolution: 4.97 Å

EMDB-66970: human ORAI1 in C2 symmetry
Method: EM (single particle) / Resolution: 4.52 Å

Source
  • Homo sapiens (human)

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