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Solid-state NMR, electrophysiology and molecular dynamics characterization of human VDAC2.

ABSTRACT: The voltage-dependent anion channel (VDAC) is the most abundant protein of the outer mitochondrial membrane and constitutes the major pathway for the transport of ADP, ATP, and other metabolites. In this multidisciplinary study we combined solid-state NMR, electrophysiology, and molecular dynamics simulations, to study the structure of the human VDAC isoform 2 in a lipid bilayer environment. We find that the structure of hVDAC2 is similar to the structure of hVDAC1, in line with recent investigations on zfVDAC2. However, hVDAC2 appears to exhibit an increased conformational heterogeneity compared to hVDAC1 which is reflected in broader solid-state NMR spectra and less defined electrophysiological profiles.

SUBMITTER: Gattin Z

PROVIDER: S-EPMC5653203 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature

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Solid-state NMR, electrophysiology and molecular dynamics characterization of human VDAC2.

Gattin Zrinka Z Schneider Robert R Laukat Yvonne Y Giller Karin K Maier Elke E Zweckstetter Markus M Griesinger Christian C Benz Roland R Becker Stefan S Lange Adam A

Journal of biomolecular NMR 20141116 3-4

The voltage-dependent anion channel (VDAC) is the most abundant protein of the outer mitochondrial membrane and constitutes the major pathway for the transport of ADP, ATP, and other metabolites. In this multidisciplinary study we combined solid-state NMR, electrophysiology, and molecular dynamics simulations, to study the structure of the human VDAC isoform 2 in a lipid bilayer environment. We find that the structure of hVDAC2 is similar to the structure of hVDAC1, in line with recent investiga ...[more]

PMID: 25399320

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