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  Electron cryo-microscopy structure of the canonical TRPC4 ion channel

Vinayagam, D., Mager, T., Apelbaum, A., Bothe, A., Merino, F., Hofnagel, O., et al. (2018). Electron cryo-microscopy structure of the canonical TRPC4 ion channel. eLife, 7: e36615. doi:10.7554/eLife.36615.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0002-C1B0-C Version Permalink: http://hdl.handle.net/21.11116/0000-0002-C1B1-B
Genre: Journal Article

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 Creators:
Vinayagam, Deivanayagabarathy1, Author              
Mager, Thomas2, Author              
Apelbaum, Amir1, Author              
Bothe, Arne1, Author              
Merino, Felipe1, Author              
Hofnagel, Oliver1, Author              
Gatsogiannis, Christos1, Author              
Raunser, Stefan1, Author              
Affiliations:
1Abt. III: Strukturbiochemie, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_2040307              
2Emeritusgruppe Biophysikalische Chemie, Max Planck Institute of Biophysics, Max Planck Society, ou_2253652              

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Free keywords: SPHIRE; TRPC; cation channel; cryo-EM; molecular biophysics; structural biology; structure; transient receptor channel; zebrafish
 Abstract: Canonical transient receptor channels (TRPC) are non-selective cation channels. They are involved in receptor-operated Ca2+ signaling and have been proposed to act as store-operated channels (SOC). Their malfunction is related to cardiomyopathies and their modulation by small molecules has been shown to be effective against renal cancer cells. The molecular mechanism underlying the complex activation and regulation is poorly understood. Here, we report the electron cryo-microscopy structure of zebrafish TRPC4 in its unliganded (apo), closed state at an overall resolution of 3.6 Å. The structure reveals the molecular architecture of the cation conducting pore, including the selectivity filter and lower gate. The cytoplasmic domain contains two key hubs that have been shown to interact with modulating proteins. Structural comparisons with other TRP channels give novel insights into the general architecture and domain organization of this superfamily of channels and help to understand their function and pharmacology.

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Language(s): eng - English
 Dates: 2018-03-122018-04-302018-05-02
 Publication Status: Published online
 Pages: 23
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.7554/eLife.36615
 Degree: -

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Title: eLife
Source Genre: Journal
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Publ. Info: Cambridge : eLife Sciences Publications
Pages: - Volume / Issue: 7 Sequence Number: e36615 Start / End Page: - Identifier: ISSN: 2050-084X
CoNE: https://pure.mpg.de/cone/journals/resource/2050-084X