Autor: |
Doreen Matthies, Chanhyung Bae, Gilman ES Toombes, Tara Fox, Alberto Bartesaghi, Sriram Subramaniam, Kenton Jon Swartz |
Jazyk: |
angličtina |
Rok vydání: |
2018 |
Předmět: |
|
Zdroj: |
eLife, Vol 7 (2018) |
Druh dokumentu: |
article |
ISSN: |
2050-084X |
DOI: |
10.7554/eLife.37558 |
Popis: |
Voltage-activated potassium (Kv) channels open to conduct K+ ions in response to membrane depolarization, and subsequently enter non-conducting states through distinct mechanisms of inactivation. X-ray structures of detergent-solubilized Kv channels appear to have captured an open state even though a non-conducting C-type inactivated state would predominate in membranes in the absence of a transmembrane voltage. However, structures for a voltage-activated ion channel in a lipid bilayer environment have not yet been reported. Here we report the structure of the Kv1.2–2.1 paddle chimera channel reconstituted into lipid nanodiscs using single-particle cryo-electron microscopy. At a resolution of ~3 Å for the cytosolic domain and ~4 Å for the transmembrane domain, the structure determined in nanodiscs is similar to the previously determined X-ray structure. Our findings show that large differences in structure between detergent and lipid bilayer environments are unlikely, and enable us to propose possible structural mechanisms for C-type inactivation. |
Databáze: |
Directory of Open Access Journals |
Externí odkaz: |
|