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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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Datensatz-Permalink: http://hdl.handle.net/21.11116/0000-0002-C1B0-C Versions-Permalink: http://hdl.handle.net/21.11116/0000-0002-C1B1-B
Genre: Zeitschriftenartikel

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 Urheber:
Vinayagam, Deivanayagabarathy1, Autor              
Mager, Thomas2, Autor              
Apelbaum, Amir1, Autor              
Bothe, Arne1, Autor              
Merino, Felipe1, Autor              
Hofnagel, Oliver1, Autor              
Gatsogiannis, Christos1, Autor              
Raunser, Stefan1, Autor              
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              

Inhalt

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Schlagwörter: SPHIRE; TRPC; cation channel; cryo-EM; molecular biophysics; structural biology; structure; transient receptor channel; zebrafish
 Zusammenfassung: 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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Sprache(n): eng - Englisch
 Datum: 2018-03-122018-04-302018-05-02
 Publikationsstatus: Online veröffentlicht
 Seiten: 23
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.7554/eLife.36615
 Art des Abschluß: -

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Titel: eLife
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: Cambridge : eLife Sciences Publications
Seiten: - Band / Heft: 7 Artikelnummer: e36615 Start- / Endseite: - Identifikator: ISSN: 2050-084X
CoNE: https://pure.mpg.de/cone/journals/resource/2050-084X