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Toward the molecular structure of the mitochondrial channel, VDAC

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Abstract

A summary is presented of the most recent information about the structure and mechanism of closure of the mitochondrial channel, VDAC. Considerable information has come from studies involving electron microscopy of two-dimensional crystals and from electrophysiological studies of wild-type channels and site-directed mutants. Available evidence points to a β-barrel as the basic structural model for VDAC. Two models for voltage- or effector- induced closure have been proposed, the first involving removal of strands from the wall of the pore, the second invoking movement of protein domains into the lumen. Experimental strategies to resolve the actual mechanism are presented.

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Authors and Affiliations

  1. Wadsworth Center for Laboratories and Research, New York State Department of Health, Empire State Plaza, P.O. Box 509, 12201-0509, Albany, New York

    Carmen A. Mannella

  2. Department of Biomedical Sciences, School of Public Health, State University of New York at Albany, 12201-0509, Albany, New York

    Carmen A. Mannella

  3. Vollum Institute for Advanced Biomedical Research, Oregon Health Sciences University, 97201, Portland, Oregon

    Michael Forte

  4. Laboratories of Cell Biology, Department of Zoology, University of Maryland, 20742, College Park, Maryland

    Marco Colombini

Authors
  1. Carmen A. Mannella
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  2. Michael Forte
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  3. Marco Colombini
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Mannella, C.A., Forte, M. & Colombini, M. Toward the molecular structure of the mitochondrial channel, VDAC. J Bioenerg Biomembr 24, 7–19 (1992). https://doi.org/10.1007/BF00769525

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