Twisting gating residues in the Orai pore
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Updated: Nov 26, 2025

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
Daniel Bonhenry1, Romana Schober2, Rainer Schindl3
1Center for Nanobiology and Structural Biology, Institute of Microbiology, Academy of Sciences of the Czech Republic, CZ-373 33, Nove Hrady, Czech Republic.
Abstract:
The store-operated calcium channels Orai1-3 form extraordinary long and funnel like pores, in stark contrast to a classical pore loop architecture. A hydrophobic segment centrally located in the Orai pore controls gating. Here, we comment on a recent work that describes decisive binding between three residues that controls the open and closed conformation of Orai channels.
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