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

被引：0

作者：

Eszter E. Najbauer

Stefan Becker

Karin Giller

Markus Zweckstetter

Adam Lange

Claudia Steinem

Bert L. de Groot

Christian Griesinger

Loren B. Andreas

机构：

[1] Max Planck Institute for Biophysical Chemistry,Department of NMR

[2] Deutsches Zentrum Für Neurodegenerative Erkrankungen (DZNE),Based Structural Biology

[3] University Medical Center Göttingen,Senior Research Group of Translational Structural Biology in Dementia

[4] University of Göttingen,Department of Neurology

[5] Leibniz-Forschungsinstitut Für Molekulare Pharmakologie,Department of Molecular Biophysics

[6] Humboldt-Universität Zu Berlin,Institut Für Biologie

[7] University of Göttingen,Institute of Organic and Biomolecular Chemistry

[8] Max-Planck Institute for Dynamics and Self-Organization,Department of Theoretical and Computational Biophysics

[9] Max-Planck Institute for Biophysical Chemistry,undefined

来源：

European Biophysics Journal | 2021年 / 50卷

关键词：

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

D O I：

暂无

中图分类号：

学科分类号：

摘要：

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.

引用

页码：159 / 172

页数：13