Structure of the human voltage-dependent anion channel
2008 | journal article; research paper. A publication with affiliation to the University of Göttingen.
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Structure of the human voltage-dependent anion channel
Bayrhuber, M.; Meins, T.; Habeck, M. ; Becker, S. ; Giller, K. ; Villinger, S. & Vonrhein, C. et al. (2008)
Proceedings of the National Academy of Sciences, 105(40) pp. 15370-15375. DOI: https://doi.org/10.1073/pnas.0808115105
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Details
- Authors
- Bayrhuber, Monika; Meins, Thomas; Habeck, Michael ; Becker, Stefan ; Giller, Karin ; Villinger, Saskia ; Vonrhein, Clemens; Griesinger, Christian ; Zweckstetter, Markus ; Zeth, Kornelius
- Abstract
- 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 beta-barrel architecture composed of 19 beta-strands with an a-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.
- Issue Date
- 2008
- Publisher
- Natl Acad Sciences
- Journal
- Proceedings of the National Academy of Sciences
- ISSN
- 0027-8424
