Twisting gating residues in the Orai pore
Language English Country Netherlands Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't, Comment
Grant support
P 28701
Austrian Science Fund FWF - Austria
PubMed
33316586
DOI
10.1016/j.ceca.2020.102323
PII: S0143-4160(20)30165-2
Knihovny.cz E-resources
- Keywords
- Ca(2+) channel, Gating, Orai1, Pore, STIM1,
- MeSH
- Ion Channel Gating * MeSH
- ORAI1 Protein genetics metabolism MeSH
- Stromal Interaction Molecule 1 metabolism MeSH
- Sulfur MeSH
- Calcium Channels * metabolism MeSH
- Publication type
- Journal Article MeSH
- Comment MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- ORAI1 Protein MeSH
- Stromal Interaction Molecule 1 MeSH
- Sulfur MeSH
- Calcium Channels * MeSH
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.
Gottfried Schatz Research Center Medical University of Graz A 8010 Graz Austria
Institute of Biophysics JKU Life Science Center Johannes Kepler University Linz A 4020 Linz Austria
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