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  Structure, gating and interactions of the voltage-dependent anion channel

Najbauer, E., Becker, S., Giller, K., Zweckstetter, M., Lange, A., Steinem, C., et al. (2021). Structure, gating and interactions of the voltage-dependent anion channel. European Biophysics Journal, 50(2), 159-172. doi:10.1007/s00249-021-01515-7.

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 Creators:
Najbauer, E.1, Author              
Becker, S.2, Author              
Giller, K.2, Author              
Zweckstetter, M.3, Author              
Lange, A.4, Author              
Steinem, C., Author
de Groot, B. L.5, Author              
Griesinger, C.2, Author              
Andreas, L. B.1, Author              
Affiliations:
1Research Group of Solid State NMR Spectroscopy-2, MPI for Biophysical Chemistry, Max Planck Society, ou_2396693              
2Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              
3Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              
4Research Group of Solid-State NMR, MPI for biophysical chemistry, Max Planck Society, ou_persistent35              
5Research Group of Computational Biomolecular Dynamics, MPI for biophysical chemistry, Max Planck Society, ou_578573              

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Free keywords: Voltage dependent anion channel; Solid-state NMR; Magic-angle spinning; Membrane protein; Electrophysiology; Molecular dynamics simulations
 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.

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Language(s): eng - English
 Dates: 2021-03-292021-03
 Publication Status: Published in print
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1007/s00249-021-01515-7
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Title: European Biophysics Journal
Source Genre: Journal
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Pages: - Volume / Issue: 50 (2) Sequence Number: - Start / End Page: 159 - 172 Identifier: -