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Structural dynamics of the human Orai1 channel revealed by cryo-electron microscopy

Year: 2026
Type: article
Abstract: 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.
Source: PLoS ONE
DOI: 10.1371/journal.pone.0348440
Authors: Yiming Zhang, Yuan Wang, Yuan Wang, Jindou Liu, Weiwei Bei, Hongkun Wang, Junli Wang, Lei Chen, Youjun Wang, Youjun Wang
Institutions: Chinese Academy of Sciences, Beijing Normal University, Institute of Biophysics, Peking University, Center for Life Sciences, State Key Laboratory of Membrane Biology, Minzu University of China
Language: English
Subfield: Sensory Systems
Open Access status: gold
Estimated APC paid: $2,382
Funders: National Natural Science Foundation of China, Chinese Academy of Sciences, Beijing Normal University, Peking University, Center for Life Sciences, Institute of Biophysics, Chinese Academy of Sciences
OpenAlex ID: W7160849593
FWCI: 11.85
Cites: 19
Cited by: 3
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