Twisting gating residues in the Orai pore.


Journal

Cell calcium
ISSN: 1532-1991
Titre abrégé: Cell Calcium
Pays: Netherlands
ID NLM: 8006226

Informations de publication

Date de publication:
01 2021
Historique:
received: 20 11 2020
revised: 23 11 2020
accepted: 23 11 2020
pubmed: 15 12 2020
medline: 3 3 2021
entrez: 14 12 2020
Statut: ppublish

Résumé

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.

Identifiants

pubmed: 33316586
pii: S0143-4160(20)30165-2
doi: 10.1016/j.ceca.2020.102323
pii:
doi:

Substances chimiques

Calcium Channels 0
ORAI1 Protein 0
Stromal Interaction Molecule 1 0
Sulfur 70FD1KFU70

Types de publication

Journal Article Research Support, Non-U.S. Gov't Comment

Langues

eng

Sous-ensembles de citation

IM

Pagination

102323

Subventions

Organisme : Austrian Science Fund FWF
ID : P 28701
Pays : Austria

Commentaires et corrections

Type : CommentOn

Informations de copyright

Copyright © 2020 Elsevier Ltd. All rights reserved.

Auteurs

Daniel Bonhenry (D)

Center for Nanobiology and Structural Biology, Institute of Microbiology, Academy of Sciences of the Czech Republic, CZ-373 33, Nove Hrady, Czech Republic.

Romana Schober (R)

Institute of Biophysics, JKU Life Science Center, Johannes Kepler University Linz, A-4020, Linz, Austria.

Rainer Schindl (R)

Gottfried Schatz Research Center, Medical University of Graz, A-8010, Graz, Austria. Electronic address: rainer.schindl@medunigraz.at.

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Classifications MeSH