A sulfur-aromatic gate latch is essential for opening of the Orai1 channel pore.

Yeung, Priscilla S-W; Ing, Christopher E; Yamashita, Megumi; Pomès, Régis; Prakriya, Murali

Yeung, Priscilla S-W; Ing, Christopher E; Yamashita, Megumi; Pomès, Régis; Prakriya, Murali.

Affiliation

Yeung PS; Department of Pharmacology, Northwestern University, Feinberg School of Medicine, Chicago, United States.
Ing CE; Molecular Medicine, Hospital for Sick Children, Toronto, Canada.
Yamashita M; Department of Biochemistry, University of Toronto, Toronto, Canada.
Pomès R; Department of Pharmacology, Northwestern University, Feinberg School of Medicine, Chicago, United States.
Prakriya M; Molecular Medicine, Hospital for Sick Children, Toronto, Canada.

Elife ; 92020 10 30.

Article in En | MEDLINE | ID: mdl-33124982

Subject(s)

Ion Channel Gating/physiology; ORAI1 Protein/metabolism; Sulfur/metabolism; HEK293 Cells; Humans; Models, Molecular; Molecular Dynamics Simulation; Mutation; Neoplasm Proteins/genetics; Neoplasm Proteins/metabolism; ORAI1 Protein/genetics; Protein Conformation; Stromal Interaction Molecule 1/genetics; Stromal Interaction Molecule 1/metabolism; Sulfur/chemistry

Key words

CRAC channels; D. melanogaster; STIM1; human; ion channel gating; molecular biophysics; orai1; store-operated calcium entry; structural biology; sulfur-aromatic interaction

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Sulfur / Ion Channel Gating / ORAI1 Protein Limits: Humans Language: En Journal: Elife Year: 2020 Type: Article Affiliation country: United States

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