Solution Structure of the Integral Human Membrane Protein VDAC-1 in Detergent Micelles
Harvard University · University of Maryland, College Park · +1 more institution
Abstract
The voltage-dependent anion channel (VDAC) mediates trafficking of small molecules and ions across the eukaryotic outer mitochondrial membrane. VDAC also interacts with antiapoptotic proteins from the Bcl-2 family, and this interaction inhibits release of apoptogenic proteins from the mitochondrion. We present the nuclear magnetic resonance (NMR) solution structure of recombinant human VDAC-1 reconstituted in detergent micelles. It forms a 19-stranded beta barrel with the first and last strand parallel. The hydrophobic outside perimeter of the barrel is covered by detergent molecules in a beltlike fashion. In the presence of cholesterol, recombinant VDAC-1 can form voltage-gated channels in phospholipid…
Citation impact
- FWCI
- 21.76
- Percentile
- 100%
- References
- 34
Authors
6- SHSebastian HillerCorresponding
Harvard University, University of Maryland, College Park, University of Gothenburg
- RGRobert Garces
Harvard University, University of Maryland, College Park, University of Gothenburg
- TMT. Malia
Harvard University, University of Maryland, College Park, University of Gothenburg
- VOVladislav Orekhov
Harvard University, University of Maryland, College Park, University of Gothenburg
- MCMarco Colombini
Harvard University, University of Maryland, College Park, University of Gothenburg
Topics & keywords
- Voltage-dependent anion channel
- Bacterial outer membrane
- Chemistry
- Micelle
- Biophysics
- Recombinant DNA
- Barrel (horology)
- Membrane protein