title: Toward the molecular structure of the mitochondrial channel, VDAC.
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 beta-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.
authors.affiliation: Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany 12201-0509.
authors.forename: C A
authors.initials: CA
authors.lastname: Mannella
authors.forename: M
authors.initials: M
authors.lastname: Forte
authors.forename: M
authors.initials: M
authors.lastname: Colombini
mesh_terms: D000595:Amino Acid Sequence; D015640:Ion Channel Gating; D007473:Ion Channels / Q000737:chemistry* / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D008928:Mitochondria / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D018272:Porins; D011487:Protein Conformation; D050994:Voltage-Dependent Anion Channels
chemical_list: D007473:Ion Channels; D008565:Membrane Proteins; D018272:Porins; D050994:Voltage-Dependent Anion Channels