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Structure of the human voltage-dependent anion channel
Open accessAbstract
The voltage-dependent anion channel (VDAC), also known as mitochondrial porin, is the most abundant protein in the mitochondrial outer membrane (MOM). VDAC is the channel known to guide the metabolic flux across the MOM and plays a key role in mitochondrially induced apoptosis. Here, we present the 3D structure of human VDAC1, which was solved conjointly by NMR spectroscopy and x-ray crystallography. Human VDAC1 (hVDAC1) adopts a β-barrel architecture composed of 19 β-strands with an α-helix located horizontally midway within the pore. Bioinformatic analysis indicates that this channel architecture is common to all VDAC proteins and is adopted by the general import pore TOM40 of mammals, which is also located in the MOM.
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“It is unlikely that VDAC itself participates as a cholesterol channel, as the center of its ring-like structure is hydrophilic, suitable for anion transport but unsuitable for hydrophobic molecule transport (103, 104).”
From Adrenal Mitochondria and Steroidogenesis: From Individual Proteins to Functional Protein Assemblies (2016) · cites this paper as [104]
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Metadata
- Authors
- Bayrhuber, M., Meins, T., Habeck, M., Becker, S., Giller, K., Villinger, S., Vonrhein, C., Griesinger, C., Zweckstetter, M., & Zeth, K.
- Affiliations
- Max Planck Institute for Biophysical Chemistry (DE)
- Max Planck Institute of Biochemistry (DE)
- Max Planck Institute for Developmental Biology (DE)
- Global Phasing (United Kingdom) (GB)
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2008-10-07
- Volume
- 105
- Issue
- 40
- Pages
- 15370-15375
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC2557026
- OpenAlex
- W2134087185
- Cited by
- 588
- References
- 37
- Citations by year
- 2026: 17 · 2025: 23 · 2024: 35 · 2023: 27 · 2022: 26 · 2021: 43 · 2020: 39 · 2019: 24 · 2018: 29 · 2017: 29 · 2016: 44 · 2015: 30 · 2014: 40 · 2013: 21 · 2012: 41
- FWCI
- 16.47
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- DORA PSI (Paul Scherrer Institute) (submittedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- GRO (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion, other-oa)
- Funders
- Deutsche Forschungsgemeinschaft (ZW 71/2-1)
- Max-Planck-Gesellschaft
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- voltage-dependent anion channel, VDAC1, mitochondrial outer membrane, protein structure, Tom40, mitochondrial apoptosis, metabolic flux
- MeSH terms
- Humans, Models, Molecular, Protein Structure, Secondary, Crystallography, X-Ray, Dimerization, Nuclear Magnetic Resonance, Biomolecular, Voltage-Dependent Anion Channel 1, Hydrophobic and Hydrophilic Interactions
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