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| Home > Publications Database > Structure, gating and interactions of the voltage-dependent anion channel. |
| Journal Article | DZNE-2021-01158 |
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2021
Springer
New York
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Please use a persistent id in citations: doi:10.1007/s00249-021-01515-7
Abstract: The voltage-dependent anion channel (VDAC) is one of the most highly abundant proteins found in the outer mitochondrial membrane, and was one of the earliest discovered. Here we review progress in understanding VDAC function with a focus on its structure, discussing various models proposed for voltage gating as well as potential drug targets to modulate the channel's function. In addition, we explore the sensitivity of VDAC structure to variations in the membrane environment, comparing DMPC-only, DMPC with cholesterol, and near-native lipid compositions, and use magic-angle spinning NMR spectroscopy to locate cholesterol on the outside of the β-barrel. We find that the VDAC protein structure remains unchanged in different membrane compositions, including conditions with cholesterol.
Keyword(s): Ion Channel Gating (MeSH) ; Molecular Dynamics Simulation (MeSH) ; Voltage-Dependent Anion Channels: chemistry (MeSH) ; Voltage-Dependent Anion Channels: metabolism (MeSH) ; Electrophysiology ; Magic-angle spinning ; Membrane protein ; Molecular dynamics simulations ; Solid-state NMR ; Voltage dependent anion channel
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